ID F1LM47_RAT Unreviewed; 465 AA. AC F1LM47; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-OCT-2019, entry version 61. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA 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., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA 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., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian 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:0000213|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., RA Lundby C., Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 RT different rat organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: ATP-specific succinyl-CoA synthetase functions in the CC citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA CC to the synthesis of ATP and thus represents the only step of CC substrate-level phosphorylation in the TCA. The beta subunit CC provides nucleotide specificity of the enzyme and binds the CC substrate succinate, while the binding sites for coenzyme A and CC phosphate are found in the alpha subunit. {ECO:0000256|HAMAP- CC 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03220}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03220}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC succinate from succinyl-CoA (ligase route): step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_03220}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta CC subunit determines specificity for ATP. {ECO:0000256|HAMAP- CC Rule:MF_03220}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP- CC Rule:MF_03220}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta CC subunit family. ATP-specific subunit beta subfamily. CC {ECO:0000256|HAMAP-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 eggNOG; COG0045; LUCA. DR GeneTree; ENSGT00390000010170; -. DR InParanoid; F1LM47; -. DR KO; K01900; -. 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 10 organ(s), highest expression level in skeletal muscle tissue. 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: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 Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_03220, KW ECO:0000256|RuleBase:RU361258}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03220}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03220}; KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03220}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03220, KW ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|RuleBase:RU361258}; KW Proteomics identification {ECO:0000213|PeptideAtlas:F1LM47}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_03220}. FT DOMAIN 63 290 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT NP_BIND 107 109 ATP. {ECO:0000256|HAMAP-Rule:MF_03220}. FT REGION 382 384 Substrate binding; shared with subunit FT alpha. {ECO:0000256|HAMAP-Rule:MF_03220}. FT METAL 260 260 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_03220}. FT METAL 274 274 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_03220}. FT BINDING 100 100 ATP. {ECO:0000256|HAMAP-Rule:MF_03220}. FT BINDING 325 325 Substrate; shared with subunit alpha. FT {ECO:0000256|HAMAP-Rule:MF_03220}. FT SITE 96 96 Important for substrate specificity. FT {ECO:0000256|HAMAP-Rule:MF_03220}. FT SITE 164 164 Important for substrate specificity. FT {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 //