ID NCPR_YEAST Reviewed; 691 AA. AC P16603; D3DKZ0; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 239. DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212}; DE Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212}; DE Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212}; DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212}; GN Name=NCP1 {ECO:0000255|HAMAP-Rule:MF_03212}; GN Synonyms=CPR1, NCPR1, PRD1; GN OrderedLocusNames=YHR042W {ECO:0000312|SGD:S000001084}; 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 PROTEIN SEQUENCE OF 2-13 AND 45-62. RX PubMed=3139648; DOI=10.1093/oxfordjournals.jbchem.a122370; RA Yabusaki Y., Murakami H., Ohkawa H.; RT "Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 RT reductase deduced from nucleotide sequence of its cloned gene."; RL J. Biochem. 103:1004-1010(1988). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION. RX PubMed=1730736; DOI=10.1016/s0021-9258(18)46051-6; RA Turi T.G., Loper J.C.; RT "Multiple regulatory elements control expression of the gene encoding the RT Saccharomyces cerevisiae cytochrome P450, lanosterol 14 alpha-demethylase RT (ERG11)."; RL J. Biol. Chem. 267:2046-2056(1992). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=9368374; DOI=10.1111/j.1574-6968.1997.tb12720.x; RA Lesuisse E., Casteras-Simon M., Labbe P.; RT "Cytochrome P-450 reductase is responsible for the ferrireductase activity RT associated with isolated plasma membranes of Saccharomyces cerevisiae."; RL FEMS Microbiol. Lett. 156:147-152(1997). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TOPOLOGY, AND RP DISRUPTION PHENOTYPE. RX PubMed=9468503; DOI=10.1074/jbc.273.8.4492; RA Venkateswarlu K., Lamb D.C., Kelly D.E., Manning N.J., Kelly S.L.; RT "The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) RT oxidoreductase is not required for catalytic activity in sterol RT biosynthesis or in reconstitution of CYP activity."; RL J. Biol. Chem. 273:4492-4496(1998). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TOPOLOGY. RX PubMed=11485306; DOI=10.1006/bbrc.2001.5338; RA Lamb D.C., Warrilow A.G., Venkateswarlu K., Kelly D.E., Kelly S.L.; RT "Activities and kinetic mechanisms of native and soluble NADPH-cytochrome RT P450 reductase."; RL Biochem. Biophys. Res. Commun. 286:48-54(2001). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [10] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [11] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=14557538; DOI=10.1073/pnas.2135500100; RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.; RT "A subset of membrane-associated proteins is ubiquitinated in response to RT mutations in the endoplasmic reticulum degradation machinery."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003). RN [12] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14576278; DOI=10.1073/pnas.2135385100; RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., RA Pfanner N., Meisinger C.; RT "The proteome of Saccharomyces cerevisiae mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003). RN [13] RP PHOSPHORYLATION, AND INTERACTION WITH PCL1. RX PubMed=15082539; DOI=10.1534/genetics.166.3.1177; RA Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.; RT "The identification of Pcl1-interacting proteins that genetically interact RT with Cla4 may indicate a link between G1 progression and mitotic exit."; RL Genetics 166:1177-1186(2004). RN [14] RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740; RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.; RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals RT accumulation of a subclass of preproteins."; RL Mol. Biol. Cell 17:1436-1450(2006). RN [15] RP FMN-BINDING AND FAD-BINDING. RX PubMed=20557022; DOI=10.1021/cb100055v; RA Ivanov A.S., Gnedenko O.V., Molnar A.A., Archakov A.I., Podust L.M.; RT "FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the RT surface is highly specific."; RL ACS Chem. Biol. 5:767-776(2010). RN [16] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 34-691 IN COMPLEX WITH FAD; FMN RP AND NADP. RX PubMed=16407065; DOI=10.1016/j.str.2005.09.015; RA Lamb D.C., Kim Y., Yermalitskaya L.V., Yermalitsky V.N., Lepesheva G.I., RA Kelly S.L., Waterman M.R., Podust L.M.; RT "A second FMN binding site in yeast NADPH-cytochrome P450 reductase RT suggests a mechanism of electron transfer by diflavin reductases."; RL Structure 14:51-61(2006). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 44-211 IN COMPLEX WITH FMN. RX PubMed=19483672; DOI=10.1038/embor.2009.82; RA Aigrain L., Pompon D., Morera S., Truan G.; RT "Structure of the open conformation of a functional chimeric NADPH RT cytochrome P450 reductase."; RL EMBO Rep. 10:742-747(2009). CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to CC cytochrome P450 in microsomes. It can also provide electron transfer to CC heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. CC Has NADPH-dependent ferrireductase activity on the plasma membrane. CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11485306, CC ECO:0000269|PubMed:1730736, ECO:0000269|PubMed:9368374, CC ECO:0000269|PubMed:9468503}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 oxidized [cytochrome P450] + NADPH = 2 reduced [cytochrome CC P450] + NADP(+) + H(+); Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, CC Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212, CC ECO:0000269|PubMed:11485306, ECO:0000269|PubMed:9368374, CC ECO:0000269|PubMed:9468503}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212, ECO:0000269|PubMed:9468503}; CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212, CC ECO:0000269|PubMed:9468503}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212, ECO:0000269|PubMed:9468503}; CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212, CC ECO:0000269|PubMed:9468503}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.59 uM for cytochrome c {ECO:0000269|PubMed:11485306}; CC KM=1.46 uM for NADPH {ECO:0000269|PubMed:11485306}; CC Note=The Vmax of the reaction is 721 pmol/min/pmol enzyme towards CC cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH. CC {ECO:0000269|PubMed:11485306}; CC -!- SUBUNIT: Interacts with PCL1. {ECO:0000269|PubMed:15082539, CC ECO:0000269|PubMed:16407065}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:9468503}; Single-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, CC ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_03212, ECO:0000305|PubMed:11485306, CC ECO:0000305|PubMed:9468503}. Mitochondrion outer membrane CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14576278, CC ECO:0000269|PubMed:16407407}; Single-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, CC ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_03212, ECO:0000305|PubMed:11485306, CC ECO:0000305|PubMed:9468503}. Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_03212, ECO:0000269|PubMed:9368374}; Single-pass membrane CC protein {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, CC ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_03212, ECO:0000305|PubMed:11485306, CC ECO:0000305|PubMed:9468503}. CC -!- INDUCTION: By galactose and on the plasma membrane by iron or copper CC deficiency. Repressed by glucose. {ECO:0000269|PubMed:9368374}. CC -!- PTM: Phosphorylated by the cyclin-CDK PCL1-PHO85. CC {ECO:0000269|PubMed:15082539}. CC -!- DISRUPTION PHENOTYPE: Accumulates 20% of ergosterol of wild type. CC {ECO:0000269|PubMed:9468503}. CC -!- MISCELLANEOUS: Present with 46600 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family. CC {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP- CC Rule:MF_03212}. 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; D13788; BAA02936.1; -; Genomic_DNA. DR EMBL; U00062; AAB68904.1; -; Genomic_DNA. DR EMBL; AY693091; AAT93110.1; -; Genomic_DNA. DR EMBL; BK006934; DAA06734.1; -; Genomic_DNA. DR PIR; S46735; S46735. DR RefSeq; NP_011908.1; NM_001179172.1. DR PDB; 2BF4; X-ray; 3.00 A; A/B=24-691. DR PDB; 2BN4; X-ray; 2.91 A; A/B=24-691. DR PDB; 2BPO; X-ray; 2.90 A; A/B=24-691. DR PDB; 3FJO; X-ray; 2.50 A; A=44-211. DR AlphaFoldDB; P16603; -. DR SMR; P16603; -. DR BioGRID; 36474; 92. DR DIP; DIP-8294N; -. DR FunCoup; P16603; 1068. DR IntAct; P16603; 15. DR MINT; P16603; -. DR STRING; 4932.YHR042W; -. DR GlyGen; P16603; 1 site. DR iPTMnet; P16603; -. DR PaxDb; 4932-YHR042W; -. DR PeptideAtlas; P16603; -. DR EnsemblFungi; YHR042W_mRNA; YHR042W; YHR042W. DR GeneID; 856438; -. DR KEGG; sce:YHR042W; -. DR AGR; SGD:S000001084; -. DR SGD; S000001084; NCP1. DR VEuPathDB; FungiDB:YHR042W; -. DR eggNOG; KOG1158; Eukaryota. DR HOGENOM; CLU_001570_17_3_1; -. DR InParanoid; P16603; -. DR OMA; QKRYQRD; -. DR OrthoDB; 1856718at2759; -. DR BioCyc; YEAST:YHR042W-MONOMER; -. DR BRENDA; 1.6.2.4; 984. DR Reactome; R-SCE-1222556; ROS and RNS production in phagocytes. DR Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation. DR Reactome; R-SCE-203615; eNOS activation. DR Reactome; R-SCE-392154; Nitric oxide stimulates guanylate cyclase. DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-SCE-5578775; Ion homeostasis. DR Reactome; R-SCE-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-SCE-9033241; Peroxisomal protein import. DR Reactome; R-SCE-9856530; High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells. DR SABIO-RK; P16603; -. DR BioGRID-ORCS; 856438; 4 hits in 10 CRISPR screens. DR EvolutionaryTrace; P16603; -. DR PRO; PR:P16603; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P16603; protein. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; EXP:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; EXP:UniProtKB. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0009055; F:electron transfer activity; IDA:SGD. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central. DR GO; GO:0010181; F:FMN binding; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:CACAO. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:SGD. DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:SGD. DR CDD; cd06204; CYPOR; 1. DR FunFam; 1.20.990.10:FF:000009; NADPH--cytochrome P450 reductase; 1. DR FunFam; 3.40.50.360:FF:000036; NADPH--cytochrome P450 reductase; 1. DR FunFam; 3.40.50.80:FF:000001; NADPH--cytochrome P450 reductase 1; 1. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 1.20.990.10; NADPH-cytochrome p450 Reductase, Chain A, domain 3; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_03212; NCPR; 1. DR InterPro; IPR003097; CysJ-like_FAD-binding. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_sf. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR023208; P450R. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1. DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000208; P450R; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PDBsum; 2BF4; -. DR PDBsum; 2BN4; -. DR PDBsum; 2BPO; -. DR PDBsum; 3FJO; -. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Direct protein sequencing; KW Endoplasmic reticulum; FAD; Flavoprotein; FMN; Isopeptide bond; KW Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion; KW Mitochondrion outer membrane; NADP; Oxidoreductase; Phosphoprotein; KW Reference proteome; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3139648" FT CHAIN 2..691 FT /note="NADPH--cytochrome P450 reductase" FT /id="PRO_0000167608" FT TOPO_DOM 2..7 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 8..24 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 25..691 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 61..204 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT DOMAIN 266..529 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 67..72 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672" FT BINDING 78 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:16407065" FT BINDING 116..119 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672" FT BINDING 152..161 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672" FT BINDING 187 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT BINDING 285 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT BINDING 439..442 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT BINDING 457..459 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT BINDING 476..479 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT BINDING 543 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT BINDING 610..611 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT BINDING 617..621 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT BINDING 646 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:16407065" FT BINDING 691 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212, FT ECO:0000269|PubMed:16407065" FT CROSSLNK 666 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT VARIANT 474 FT /note="V -> G" FT CONFLICT 423 FT /note="T -> N (in Ref. 1; BAA02936)" FT /evidence="ECO:0000305" FT HELIX 50..56 FT /evidence="ECO:0007829|PDB:3FJO" FT STRAND 60..66 FT /evidence="ECO:0007829|PDB:3FJO" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 71..87 FT /evidence="ECO:0007829|PDB:3FJO" FT STRAND 91..95 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:3FJO" FT STRAND 109..116 FT /evidence="ECO:0007829|PDB:3FJO" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 128..136 FT /evidence="ECO:0007829|PDB:3FJO" FT TURN 139..144 FT /evidence="ECO:0007829|PDB:3FJO" FT STRAND 146..153 FT /evidence="ECO:0007829|PDB:3FJO" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 162..173 FT /evidence="ECO:0007829|PDB:3FJO" FT STRAND 183..186 FT /evidence="ECO:0007829|PDB:3FJO" FT TURN 187..190 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 192..210 FT /evidence="ECO:0007829|PDB:3FJO" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 223..226 FT /evidence="ECO:0007829|PDB:2BN4" FT STRAND 234..239 FT /evidence="ECO:0007829|PDB:2BN4" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 271..278 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 287..293 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 306..309 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 315..325 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 348..351 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 352..358 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 365..367 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 368..374 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 375..377 FT /evidence="ECO:0007829|PDB:2BN4" FT HELIX 381..390 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 394..400 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 402..404 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 408..416 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 426..432 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:2BN4" FT STRAND 439..443 FT /evidence="ECO:0007829|PDB:2BPO" FT TURN 447..449 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 453..459 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:2BF4" FT HELIX 477..489 FT /evidence="ECO:0007829|PDB:2BPO" FT TURN 494..496 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 508..510 FT /evidence="ECO:0007829|PDB:2BPO" FT TURN 511..515 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 519..522 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 536..541 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 542..545 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 546..560 FT /evidence="ECO:0007829|PDB:2BPO" FT TURN 564..566 FT /evidence="ECO:0007829|PDB:2BN4" FT HELIX 570..573 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 574..585 FT /evidence="ECO:0007829|PDB:2BPO" FT TURN 587..591 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 592..599 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 600..602 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 603..610 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 620..626 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 628..635 FT /evidence="ECO:0007829|PDB:2BPO" FT TURN 636..638 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 640..645 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 650..665 FT /evidence="ECO:0007829|PDB:2BPO" FT HELIX 670..682 FT /evidence="ECO:0007829|PDB:2BPO" FT STRAND 685..690 FT /evidence="ECO:0007829|PDB:2BPO" SQ SEQUENCE 691 AA; 76772 MW; 82BB847701E5438B CRC64; MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI AQVVTENNKN YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD FESLNDVPVI VSIFISTYGE GDFPDGAVNF EDFICNAEAG ALSNLRYNMF GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG KLGEADDGAG TTDEDYMAWK DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE PSAHYLPSHQ LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT TIGAAIKHYL EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE ITSKYFNIAD ALKYLSDGAK WDTVPMQFLV ESVPQMTPRY YSISSSSLSE KQTVHVTSIV ENFPNPELPD APPVVGVTTN LLRNIQLAQN NVNIAETNLP VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG PGTGVAPFRG FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM AKGVSTALVG ILSRGKSITT DEATELIKML KTSGRYQEDV W //