ID ATG7_YEAST Reviewed; 630 AA. AC P38862; D3DLC0; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 04-NOV-2026, entry version 203. DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7; DE AltName: Full=ATG12-activating enzyme E1 ATG7; DE AltName: Full=Autophagy-related protein 7; DE AltName: Full=Cytoplasm to vacuole targeting protein 2; GN Name=ATG7; Synonyms=APG7, CVT2; OrderedLocusNames=YHR171W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=ATCC 26109 / X2180; RX PubMed=9759731; DOI=10.1038/26506; RA Mizushima N., Noda T., Yoshimori T., Tanaka Y., Ishii T., George M.D., RA Klionsky D.J., Ohsumi M., Ohsumi Y.; RT "A protein conjugation system essential for autophagy."; RL Nature 395:395-398(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8091229; DOI=10.1126/science.8091229; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., RA Waterston R., Wilson R., Vaudin M.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT VIII."; RL Science 265:2077-2082(1994). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP FUNCTION. RX PubMed=8224160; DOI=10.1016/0014-5793(93)80398-e; RA Tsukada M., Ohsumi Y.; RT "Isolation and characterization of autophagy-defective mutants of RT Saccharomyces cerevisiae."; RL FEBS Lett. 333:169-174(1993). RN [5] RP FUNCTION. RX PubMed=7593182; DOI=10.1083/jcb.131.3.591; RA Harding T.M., Morano K.A., Scott S.V., Klionsky D.J.; RT "Isolation and characterization of yeast mutants in the cytoplasm to RT vacuole protein targeting pathway."; RL J. Cell Biol. 131:591-602(1995). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10233148; DOI=10.1091/mbc.10.5.1337; RA Kim J., Dalton V.M., Eggerton K.P., Scott S.V., Klionsky D.J.; RT "Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, RT macroautophagy, and peroxisome degradation pathways."; RL Mol. Biol. Cell 10:1337-1351(1999). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG12, AND MUTAGENESIS OF RP GLY-333 AND CYS-507. RX PubMed=10233150; DOI=10.1091/mbc.10.5.1367; RA Tanida I., Mizushima N., Kiyooka M., Ohsumi M., Ueno T., Ohsumi Y., RA Kominami E.; RT "Apg7p/Cvt2p: a novel protein-activating enzyme essential for autophagy."; RL Mol. Biol. Cell 10:1367-1379(1999). RN [8] RP FUNCTION, INTERACTION WITH ATG8, AND MUTAGENESIS OF GLY-333 AND CYS-507. RX PubMed=11100732; DOI=10.1038/35044114; RA Ichimura Y., Kirisako T., Takao T., Satomi Y., Shimonishi Y., Ishihara N., RA Mizushima N., Tanida I., Kominami E., Ohsumi M., Noda T., Ohsumi Y.; RT "A ubiquitin-like system mediates protein lipidation."; RL Nature 408:488-492(2000). RN [9] RP HOMODIMERIZATION, AND INTERACTION WITH ATG3; ATG8 AND ATG12. RX PubMed=11139573; DOI=10.1074/jbc.m007737200; RA Komatsu M., Tanida I., Ueno T., Ohsumi M., Ohsumi Y., Kominami E.; RT "The C-terminal region of an Apg7p/Cvt2p is required for homodimerization RT and is essential for its E1 activity and E1-E2 complex formation."; RL J. Biol. Chem. 276:9846-9854(2001). RN [10] RP FUNCTION. RX PubMed=11149920; DOI=10.1083/jcb.152.1.51; RA Kim J., Huang W.-P., Klionsky D.J.; RT "Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole RT targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation RT complex."; RL J. Cell Biol. 152:51-64(2001). RN [11] RP NOMENCLATURE. RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x; RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y., RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.; RT "A unified nomenclature for yeast autophagy-related genes."; RL Dev. Cell 5:539-545(2003). RN [12] RP FUNCTION. RX PubMed=12965207; DOI=10.1016/s0014-5793(03)00899-8; RA Yamazaki-Sato H., Tanida I., Ueno T., Kominami E.; RT "The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8 RT lipidation, but not for Apg12 conjugation."; RL FEBS Lett. 551:71-77(2003). RN [13] RP FUNCTION, AND MUTAGENESIS OF CYS-507. RX PubMed=15277523; DOI=10.1074/jbc.m405860200; RA Ichimura Y., Imamura Y., Emoto K., Umeda M., Noda T., Ohsumi Y.; RT "In vivo and in vitro reconstitution of atg8 conjugation essential for RT autophagy."; RL J. Biol. Chem. 279:40584-40592(2004). RN [14] RP INTERACTION WITH ATG12. RX PubMed=16874032; DOI=10.4161/auto.1.2.1858; RA Hanada T., Ohsumi Y.; RT "Structure-function relationship of Atg12, a ubiquitin-like modifier RT essential for autophagy."; RL Autophagy 1:110-118(2005). RN [15] RP FUNCTION. RX PubMed=16027116; DOI=10.1074/jbc.m506736200; RA Onodera J., Ohsumi Y.; RT "Autophagy is required for maintenance of amino acid levels and protein RT synthesis under nitrogen starvation."; RL J. Biol. Chem. 280:31582-31586(2005). RN [16] RP FUNCTION. RX PubMed=17632063; DOI=10.1016/j.cell.2007.05.021; RA Nakatogawa H., Ichimura Y., Ohsumi Y.; RT "Atg8, a ubiquitin-like protein required for autophagosome formation, RT mediates membrane tethering and hemifusion."; RL Cell 130:165-178(2007). RN [17] RP FUNCTION. RX PubMed=17890363; DOI=10.1534/genetics.107.076596; RA Ma J., Jin R., Jia X., Dobry C.J., Wang L., Reggiori F., Zhu J., Kumar A.; RT "An interrelationship between autophagy and filamentous growth in budding RT yeast."; RL Genetics 177:205-214(2007). RN [18] RP INTERACTION WITH ATG3. RX PubMed=17227760; DOI=10.1074/jbc.m611473200; RA Yamada Y., Suzuki N.N., Hanada T., Ichimura Y., Kumeta H., Fujioka Y., RA Ohsumi Y., Inagaki F.; RT "The crystal structure of Atg3, an autophagy-related ubiquitin carrier RT protein (E2) enzyme that mediates Atg8 lipidation."; RL J. Biol. Chem. 282:8036-8043(2007). RN [19] RP SUBCELLULAR LOCATION. RX PubMed=18497569; DOI=10.4161/auto.6308; RA Ma J., Bharucha N., Dobry C.J., Frisch R.L., Lawson S., Kumar A.; RT "Localization of autophagy-related proteins in yeast using a versatile RT plasmid-based resource of fluorescent protein fusions."; RL Autophagy 4:792-800(2008). RN [20] RP FUNCTION, AND INTERACTION WITH ATG8. RX PubMed=18544538; DOI=10.1074/jbc.m801836200; RA Oh-oka K., Nakatogawa H., Ohsumi Y.; RT "Physiological pH and acidic phospholipids contribute to substrate RT specificity in lipidation of Atg8."; RL J. Biol. Chem. 283:21847-21852(2008). RN [21] RP FUNCTION. RX PubMed=18725539; DOI=10.1083/jcb.200801035; RA Cao Y., Cheong H., Song H., Klionsky D.J.; RT "In vivo reconstitution of autophagy in Saccharomyces cerevisiae."; RL J. Cell Biol. 182:703-713(2008). RN [22] RP FUNCTION. RX PubMed=18701704; DOI=10.1091/mbc.e08-04-0363; RA Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L., RA Millen J., Goldfarb D.S., Thumm M.; RT "Piecemeal microautophagy of the nucleus requires the core macroautophagy RT genes."; RL Mol. Biol. Cell 19:4492-4505(2008). RN [23] RP FUNCTION. RX PubMed=19302372; DOI=10.1111/j.1474-9726.2009.00469.x; RA Alvers A.L., Fishwick L.K., Wood M.S., Hu D., Chung H.S., Dunn W.A. Jr., RA Aris J.P.; RT "Autophagy and amino acid homeostasis are required for chronological RT longevity in Saccharomyces cerevisiae."; RL Aging Cell 8:353-369(2009). RN [24] RP FUNCTION. RX PubMed=19061865; DOI=10.1016/j.bbrc.2008.11.084; RA Kageyama T., Suzuki K., Ohsumi Y.; RT "Lap3 is a selective target of autophagy in yeast, Saccharomyces RT cerevisiae."; RL Biochem. Biophys. Res. Commun. 378:551-557(2009). RN [25] RP SUBUNIT. RX PubMed=21193819; DOI=10.4014/jmb.1007.07061; RA Bae J.Y., Park H.H.; RT "Purification and characterization of a ubiquitin-like system for RT autophagosome formation."; RL J. Microbiol. Biotechnol. 20:1647-1652(2010). RN [26] RP FUNCTION. RX PubMed=22785534; DOI=10.1038/cddis.2012.90; RA Clapp C., Portt L., Khoury C., Sheibani S., Norman G., Ebner P., Eid R., RA Vali H., Mandato C.A., Madeo F., Greenwood M.T.; RT "14-3-3 protects against stress-induced apoptosis."; RL Cell Death Dis. 3:E348-E348(2012). RN [27] RP FUNCTION. RX PubMed=22768199; DOI=10.1371/journal.pone.0040013; RA Mijaljica D., Prescott M., Devenish R.J.; RT "A late form of nucleophagy in Saccharomyces cerevisiae."; RL PLoS ONE 7:E40013-E40013(2012). RN [28] RP FUNCTION. RX PubMed=23660403; DOI=10.1016/j.febslet.2013.04.030; RA Eiyama A., Kondo-Okamoto N., Okamoto K.; RT "Mitochondrial degradation during starvation is selective and temporally RT distinct from bulk autophagy in yeast."; RL FEBS Lett. 587:1787-1792(2013). RN [29] RP FUNCTION, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-507; ARG-511 AND RP GLU-524. RX PubMed=29295865; DOI=10.1096/fj.201701057r; RA Mashahreh B., Hassouna F., Soudah N., Cohen-Kfir E., Strulovich R., RA Haitin Y., Wiener R.; RT "Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP RT binding."; RL FASEB J. 32:2794-2802(2018). RN [30] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=22055190; DOI=10.1016/j.molcel.2011.08.034; RA Taherbhoy A.M., Tait S.W., Kaiser S.E., Williams A.H., Deng A., Nourse A., RA Hammel M., Kurinov I., Rock C.O., Green D.R., Schulman B.A.; RT "Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and RT mechanism in the autophagy pathway."; RL Mol. Cell 44:451-461(2011). RN [31] RP STRUCTURE BY NMR OF 601-630 IN COMPLEX WITH ATG8, X-RAY CRYSTALLOGRAPHY IN RP COMPLEX WITH ARG8, FUNCTION, AND MUTAGENESIS OF ARG-443; SER-466; TYR-486; RP ASP-490 AND ARG-550. RX PubMed=22055191; DOI=10.1016/j.molcel.2011.08.035; RA Noda N.N., Satoo K., Fujioka Y., Kumeta H., Ogura K., Nakatogawa H., RA Ohsumi Y., Inagaki F.; RT "Structural basis of Atg8 activation by a homodimeric E1, Atg7."; RL Mol. Cell 44:462-475(2011). RN [32] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ATG8, AND INTERACTION WITH ATG3. RX PubMed=22056771; DOI=10.1038/nsmb.2165; RA Hong S.B., Kim B.W., Lee K.E., Kim S.W., Jeon H., Kim J., Song H.K.; RT "Insights into noncanonical E1 enzyme activation from the structure of RT autophagic E1 Atg7 with Atg8."; RL Nat. Struct. Mol. Biol. 18:1323-1330(2011). RN [33] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ATG3 AND ATG10. RX PubMed=23142976; DOI=10.1038/nsmb.2415; RA Kaiser S.E., Mao K., Taherbhoy A.M., Yu S., Olszewski J.L., Duda D.M., RA Kurinov I., Deng A., Fenn T.D., Klionsky D.J., Schulman B.A.; RT "Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and RT Atg7-Atg10 structures."; RL Nat. Struct. Mol. Biol. 19:1242-1249(2012). CC -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like CC systems required for cytoplasm to vacuole transport (Cvt) and CC autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for CC its conjugation with phosphatidylethanolamine. Both systems are needed CC for the ATG8 association to Cvt vesicles and autophagosomes membranes. CC Autophagy is essential for maintenance of amino acid levels and protein CC synthesis under nitrogen starvation. Required for selective autophagic CC degradation of the nucleus (nucleophagy) as well as for mitophagy which CC contributes to regulate mitochondrial quantity and quality by CC eliminating the mitochondria to a basal level to fulfill cellular CC energy requirements and preventing excess ROS production. Plays a role CC in the regulation of filamentous growth and chronological longevity. CC {ECO:0000269|PubMed:10233148, ECO:0000269|PubMed:10233150, CC ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:11149920, CC ECO:0000269|PubMed:12965207, ECO:0000269|PubMed:15277523, CC ECO:0000269|PubMed:16027116, ECO:0000269|PubMed:17632063, CC ECO:0000269|PubMed:17890363, ECO:0000269|PubMed:18544538, CC ECO:0000269|PubMed:18701704, ECO:0000269|PubMed:18725539, CC ECO:0000269|PubMed:19061865, ECO:0000269|PubMed:19302372, CC ECO:0000269|PubMed:22055191, ECO:0000269|PubMed:22768199, CC ECO:0000269|PubMed:22785534, ECO:0000269|PubMed:23660403, CC ECO:0000269|PubMed:29295865, ECO:0000269|PubMed:7593182, CC ECO:0000269|PubMed:8224160, ECO:0000269|PubMed:9759731}. CC -!- SUBUNIT: Homodimer; homodimerization is required for ATP-binding CC (PubMed:11139573, PubMed:21193819, PubMed:29295865). Interacts with CC ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly- CC 116' of ATG8 and with ATG12 through a thioester bond between Cys-507 CC and the C-terminal 'Gly-186' of ATG12 (PubMed:10233150, CC PubMed:11100732, PubMed:16874032, PubMed:18544538, PubMed:22055191). CC Also interacts with ATG3 (PubMed:11139573, PubMed:17227760, CC PubMed:22056771, PubMed:23142976). {ECO:0000269|PubMed:10233150, CC ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:11139573, CC ECO:0000269|PubMed:16874032, ECO:0000269|PubMed:17227760, CC ECO:0000269|PubMed:18544538, ECO:0000269|PubMed:21193819, CC ECO:0000269|PubMed:22055191, ECO:0000269|PubMed:22056771, CC ECO:0000269|PubMed:23142976, ECO:0000269|PubMed:29295865}. CC -!- INTERACTION: CC P38862; Q07879: ATG10; NbExp=7; IntAct=EBI-2677, EBI-36629; CC P38862; P40344: ATG3; NbExp=10; IntAct=EBI-2677, EBI-3381; CC P38862; P38862: ATG7; NbExp=3; IntAct=EBI-2677, EBI-2677; CC P38862; P38182: ATG8; NbExp=12; IntAct=EBI-2677, EBI-2684; CC P38862; Q9GZQ8: MAP1LC3B; Xeno; NbExp=2; IntAct=EBI-2677, EBI-373144; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure. CC -!- DOMAIN: The C-terminal 40 residues are required for homodimerization, CC as well as the interactions with ATG3, ATG8 and ATG12; and the C- CC terminal 17 residues are required for the ATG8 lipidation. CC -!- DOMAIN: The GxGxxG motif is important for the function, possibly CC through binding with ATP. CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB017925; BAA33474.1; -; Genomic_DNA. DR EMBL; U00027; AAB68016.1; -; Genomic_DNA. DR EMBL; BK006934; DAA06864.1; -; Genomic_DNA. DR PIR; S48910; S48910. DR RefSeq; NP_012041.1; NM_001179302.1. DR PDB; 2LI5; NMR; -; B=601-630. DR PDB; 3RUI; X-ray; 1.91 A; A=293-630. DR PDB; 3RUJ; X-ray; 2.10 A; A=1-294. DR PDB; 3T7E; X-ray; 2.25 A; A=289-630. DR PDB; 3T7F; X-ray; 1.89 A; A=1-289. DR PDB; 3T7G; X-ray; 2.08 A; A/B=1-289. DR PDB; 3T7H; X-ray; 1.60 A; A/B=1-289. DR PDB; 3VH1; X-ray; 3.00 A; A=1-595. DR PDB; 3VH2; X-ray; 3.30 A; A=1-613. DR PDB; 3VH3; X-ray; 2.00 A; A=295-630. DR PDB; 3VH4; X-ray; 2.65 A; A=295-630. DR PDB; 4GSJ; X-ray; 1.70 A; A=1-289. DR PDB; 4GSK; X-ray; 2.90 A; A/B=1-613. DR PDB; 4GSL; X-ray; 2.70 A; A/B=1-613. DR PDB; 5YEC; X-ray; 2.15 A; A/C=295-630. DR AlphaFoldDB; P38862; -. DR BMRB; P38862; -. DR MDRepo; P38862; -. DR SMR; P38862; -. DR BioGRID; 36605; 128. DR DIP; DIP-1196N; -. DR FunCoup; P38862; 872. DR IntAct; P38862; 8. DR STRING; 4932.YHR171W; -. DR GlyGen; P38862; 1 site. DR iPTMnet; P38862; -. DR PaxDb; 4932-YHR171W; -. DR PeptideAtlas; P38862; -. DR TopDownProteomics; P38862; -. DR EnsemblFungi; YHR171W_mRNA; YHR171W; YHR171W. DR GeneID; 856576; -. DR KEGG; sce:YHR171W; -. DR AGR; SGD:S000001214; -. DR SGD; S000001214; ATG7. DR VEuPathDB; FungiDB:YHR171W; -. DR eggNOG; KOG2337; Eukaryota. DR HOGENOM; CLU_012998_2_1_1; -. DR InParanoid; P38862; -. DR OMA; AACNDWR; -. DR OrthoDB; 338614at2759; -. DR BioCyc; YEAST:G3O-31205-MONOMER; -. DR Reactome; R-SCE-1632852; Macroautophagy. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 856576; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P38862; -. DR PRO; PR:P38862; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P38862; protein. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD. DR GO; GO:0019778; F:Atg12 activating enzyme activity; IMP:SGD. DR GO; GO:0019779; F:Atg8 activating enzyme activity; IMP:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central. DR GO; GO:0006914; P:autophagy; IMP:SGD. DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD. DR GO; GO:0006501; P:C-terminal protein lipidation; IDA:SGD. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central. DR GO; GO:0032258; P:cytoplasm to vacuole targeting by the Cvt pathway; IMP:SGD. DR GO; GO:0016236; P:macroautophagy; IMP:SGD. DR GO; GO:0000423; P:mitophagy; IBA:GO_Central. DR GO; GO:0044804; P:nucleophagy; IMP:SGD. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD. DR GO; GO:0032446; P:protein modification by small protein conjugation; IMP:SGD. DR CDD; cd01486; Apg7; 1. DR DisProt; DP02249; -. DR FunFam; 3.40.50.720:FF:000243; Ubiquitin-like modifier-activating enzyme ATG7; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.40.140.100; Ubiquitin-like modifier-activating enzyme ATG7 C-terminal domain; 1. DR Gene3D; 3.40.140.70; Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain; 1. DR InterPro; IPR006285; Atg7. DR InterPro; IPR032197; Atg7_N. DR InterPro; IPR042522; Atg7_N_1. DR InterPro; IPR042523; Atg7_N_2. DR InterPro; IPR045886; ThiF/MoeB/HesA. DR InterPro; IPR000594; ThiF_NAD_FAD-bd. DR InterPro; IPR035985; Ubiquitin-activating_enz. DR NCBIfam; TIGR01381; E1_like_apg7; 1. DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1. DR PANTHER; PTHR10953:SF3; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME ATG7; 1. DR Pfam; PF16420; ATG7_N; 1. DR Pfam; PF00899; ThiF; 1. DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1. PE 1: Evidence at protein level; KW 3D-structure; Autophagy; Cytoplasm; Protein transport; Reference proteome; KW Transport; Ubl conjugation pathway. FT CHAIN 1..630 FT /note="Ubiquitin-like modifier-activating enzyme ATG7" FT /id="PRO_0000212822" FT REGION 591..630 FT /note="Homodimerization" FT MOTIF 331..336 FT /note="GXGXXG motif" FT ACT_SITE 507 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000269|PubMed:29295865" FT MUTAGEN 333 FT /note="G->A: Loss of interaction with ATG8 and ATG12, and FT no more ATG12-ATG5 conjugate. Defect in Cvt pathway and FT autophagy." FT /evidence="ECO:0000269|PubMed:10233150, FT ECO:0000269|PubMed:11100732" FT MUTAGEN 443 FT /note="R->A: Loss of interaction with ATG8." FT /evidence="ECO:0000269|PubMed:22055191" FT MUTAGEN 466 FT /note="S->A: Loss of interaction with ATG8; when associated FT with F-486 and A-490." FT /evidence="ECO:0000269|PubMed:22055191" FT MUTAGEN 486 FT /note="Y->F: Loss of interaction with ATG8; when associated FT with A-466 and A-490." FT /evidence="ECO:0000269|PubMed:22055191" FT MUTAGEN 490 FT /note="D->A: Loss of interaction with ATG8; when associated FT with A-466 and F-486." FT /evidence="ECO:0000269|PubMed:22055191" FT MUTAGEN 507 FT /note="C->A: Loss of interaction with ATG8 and ATG12 and no FT more formation of ATG12-ATG5 conjugate. Defect in Cvt FT pathway and autophagy." FT /evidence="ECO:0000269|PubMed:10233150, FT ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:15277523, FT ECO:0000269|PubMed:29295865" FT MUTAGEN 507 FT /note="C->S: Instead of the formation of an intermediate FT complex with a thiol ester bond between ATG7 (E1-like FT enzyme) and ATG8 (substrate) or between ATG7 and ATG12 FT (substrate), a stable complex with an O-ester bond is FT formed. No more formation of ATG12-ATG5 conjugate." FT /evidence="ECO:0000269|PubMed:10233150, FT ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:15277523" FT MUTAGEN 511 FT /note="R->A: Impaired homodimerization and ATP-binding. FT Homodimerization and ATP-binding are recovered when it FT heterodimerizes with an ATG7 molecule with a R-524 FT mutation." FT /evidence="ECO:0000269|PubMed:29295865" FT MUTAGEN 524 FT /note="E->R: Impaired homodimerization and ATP-binding. FT Homodimerization and ATP-binding are recovered when it FT heterodimerizes with an ATG7 molecule with a A-511 FT mutation." FT /evidence="ECO:0000269|PubMed:29295865" FT MUTAGEN 550 FT /note="R->A: Loss of interaction with ATG8." FT /evidence="ECO:0000269|PubMed:22055191" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 19..29 FT /evidence="ECO:0007829|PDB:3T7H" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:3T7G" FT STRAND 36..46 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:3VH2" FT STRAND 56..62 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:4GSL" FT STRAND 78..89 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 90..95 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 98..113 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 123..130 FT /evidence="ECO:0007829|PDB:3T7H" FT TURN 131..134 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 135..148 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 151..157 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 159..164 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 165..174 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 194..200 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 219..229 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 248..256 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:3T7F" FT STRAND 269..273 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:3T7H" FT STRAND 284..287 FT /evidence="ECO:0007829|PDB:3T7H" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:3RUJ" FT HELIX 294..308 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 309..313 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 319..323 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 326..330 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 334..345 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 350..354 FT /evidence="ECO:0007829|PDB:3RUI" FT TURN 364..366 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 376..378 FT /evidence="ECO:0007829|PDB:3VH1" FT HELIX 379..390 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:4GSK" FT STRAND 395..399 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 402..405 FT /evidence="ECO:0007829|PDB:3VH4" FT HELIX 413..429 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 431..435 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:3VH4" FT HELIX 441..443 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 444..452 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 456..462 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 464..471 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 486..489 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 490..492 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:3VH1" FT TURN 498..500 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 504..508 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 512..529 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 537..540 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 547..552 FT /evidence="ECO:0007829|PDB:3RUI" FT TURN 553..556 FT /evidence="ECO:0007829|PDB:3RUI" FT STRAND 557..561 FT /evidence="ECO:0007829|PDB:3RUI" FT TURN 570..572 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 574..583 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 585..593 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 595..602 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 604..612 FT /evidence="ECO:0007829|PDB:3RUI" FT HELIX 616..618 FT /evidence="ECO:0007829|PDB:2LI5" FT HELIX 627..629 FT /evidence="ECO:0007829|PDB:2LI5" SQ SEQUENCE 630 AA; 71428 MW; 561EEC94F0ED57F5 CRC64; MSSERVLSYA PAFKSFLDTS FFQELSRLKL DVLKLDSTCQ PLTVNLDLHN IPKSADQVPL FLTNRSFEKH NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL FLHQRALECW EDGIKDINKC VSFVIISFAD LKKYRFYYWL GVPCFQRPSS TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV CILDADDEIV NYDKCIIRKT KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI IRQNEGSFAL NATFASIDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK ITFVDNGTVS YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK LSIPMIGHKL VNEEAQHKDF DRLRALIKEH DIIFLLVDSR ESRWLPSLLS NIENKTVINA ALGFDSYLVM RHGNRDEQSS KQLGCYFCHD VVAPTDSLTD RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT VLGDIPHQIR GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE ISGLSVIKQE VERLGNDVFE WEDDESDEIA //