ID F1LM47_RAT Unreviewed; 465 AA. AC F1LM47; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-SEP-2021, entry version 69. DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03220}; DE EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_03220}; DE AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_03220}; DE Short=A-SCS {ECO:0000256|HAMAP-Rule:MF_03220}; DE AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000256|HAMAP-Rule:MF_03220}; DE Short=SCS-betaA {ECO:0000256|HAMAP-Rule:MF_03220}; GN Name=Sucla2 {ECO:0000313|Ensembl:ENSRNOP00000060229, GN ECO:0000313|RGD:1309397}; GN Synonyms=SUCLA2 {ECO:0000256|HAMAP-Rule:MF_03220}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000060229, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000060229, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060229, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000060229} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060229}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0007829|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: ATP-specific succinyl-CoA synthetase functions in the citric CC acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the CC synthesis of ATP and thus represents the only step of substrate-level CC phosphorylation in the TCA. The beta subunit provides nucleotide CC specificity of the enzyme and binds the substrate succinate, while the CC binding sites for coenzyme A and phosphate are found in the alpha CC subunit. {ECO:0000256|HAMAP-Rule:MF_03220}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; CC Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, CC ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03220}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03220}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03220}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate CC from succinyl-CoA (ligase route): step 1/1. CC {ECO:0000256|ARBA:ARBA00005064, ECO:0000256|HAMAP-Rule:MF_03220}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit CC determines specificity for ATP. {ECO:0000256|HAMAP-Rule:MF_03220}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03220}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit CC family. ATP-specific subunit beta subfamily. {ECO:0000256|HAMAP- CC Rule:MF_03220}. 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; AABR07018391; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07018392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07018393; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001101857.2; NM_001108387.2. DR SMR; F1LM47; -. DR STRING; 10116.ENSRNOP00000060229; -. DR jPOST; F1LM47; -. DR PaxDb; F1LM47; -. DR PRIDE; F1LM47; -. DR Ensembl; ENSRNOT00000065195; ENSRNOP00000060229; ENSRNOG00000017481. DR GeneID; 361071; -. DR KEGG; rno:361071; -. DR CTD; 8803; -. DR RGD; 1309397; Sucla2. DR eggNOG; KOG2799; Eukaryota. DR GeneTree; ENSGT00390000010170; -. DR HOGENOM; CLU_037430_0_0_1; -. DR InParanoid; F1LM47; -. DR OMA; ITACDEV; -. DR OrthoDB; 973871at2759; -. DR TreeFam; TF300624; -. DR Reactome; R-RNO-71403; Citric acid cycle (TCA cycle). DR UniPathway; UPA00223; UER00999. DR Proteomes; UP000002494; Chromosome 15. DR Bgee; ENSRNOG00000017481; Expressed in quadriceps femoris and 21 other tissues. DR Genevisible; F1LM47; RN. DR GO; GO:0005739; C:mitochondrion; IDA:RGD. DR GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IDA:RGD. DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central. DR GO; GO:0006105; P:succinate metabolic process; IDA:RGD. DR GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:RGD. DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:RGD. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.40.50.261; -; 1. DR HAMAP; MF_00558; Succ_CoA_beta; 1. DR HAMAP; MF_03220; Succ_CoA_betaA_euk; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR005811; CoA_ligase. DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS. DR InterPro; IPR034723; Succ_CoA_betaA_euk. DR InterPro; IPR005809; Succ_CoA_synthase_bsu. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR PANTHER; PTHR11815; PTHR11815; 1. DR Pfam; PF08442; ATP-grasp_2; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001554; SucCS_beta; 1. DR SUPFAM; SSF52210; SSF52210; 1. DR TIGRFAMs; TIGR01016; sucCoAbeta; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03220, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03220}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03220}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03220}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP- KW Rule:MF_03220}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03220}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F1LM47}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_03220}. FT DOMAIN 63..290 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT NP_BIND 107..109 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT REGION 382..384 FT /note="Substrate binding; shared with subunit alpha" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT METAL 260 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT METAL 274 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT BINDING 100 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT BINDING 325 FT /note="Substrate; shared with subunit alpha" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT SITE 96 FT /note="Important for substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT SITE 164 FT /note="Important for substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" SQ SEQUENCE 465 AA; 50306 MW; 4A148D18475E621D CRC64; MAASMFFGRQ LAAAALRSHR SQTTVRATAQ ALGSSGLFNK HGFQMQQQQQ QQRSLSLHEY LSMELLQEAG VSVPKGFVAK SSDEAYAIAK KLGSKDVVIK AQVLAGGRGK GTFTSGLKGG VKIVFSPEEA KAVSSQMIGQ KLITKQTGAK GRICNQVLVC ERKYPRREYY FAITMERSFQ GPVLIGSSQG GVNIEDVAAE NPEAIVKEPV DIIEGVKKEQ AVTLAKKMGF PSNIVDSAAE NMIKLYNLFL KYDATMVEIN PMVEDADGKV LCMDAKINFD SNSAYRQKKI FALQDWSQED ERDKDAADAD INYIGLDGNI GCLVNGAGLA MATMDIIKLH GGTPANFLDV GGGATVHQVT EAFKLITSDK RVQAILVNIF GGIMRCDIIA QGIVMAVKDL EIRIPVVVRL QGTRVDDAKA LIADSGLKIL ACDDLDEAAK MVVKLSEIVT LAKEAHVDVK FQLPI //