ID F1LM47_RAT Unreviewed; 465 AA. AC F1LM47; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 13-SEP-2023, entry version 77. 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:ENSRNOP00000060229.1, 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:ENSRNOP00000060229.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000060229.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060229.1, 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: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). RN [3] {ECO:0000313|Ensembl:ENSRNOP00000060229.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060229.1}; RG Ensembl; RL Submitted (MAY-2023) to UniProtKB. 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 RefSeq; NP_001101857.2; NM_001108387.2. DR AlphaFoldDB; F1LM47; -. DR SMR; F1LM47; -. DR STRING; 10116.ENSRNOP00000060229; -. DR GlyGen; F1LM47; 3 sites, 1 O-linked glycan (3 sites). DR jPOST; F1LM47; -. DR PaxDb; F1LM47; -. DR Ensembl; ENSRNOT00000065195.4; ENSRNOP00000060229.1; ENSRNOG00000017481.7. DR GeneID; 361071; -. DR KEGG; rno:361071; -. DR AGR; RGD:1309397; -. 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; 1384037at2759; -. 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 20 other tissues. DR Genevisible; F1LM47; RN. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central. DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); ISO:RGD. 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; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 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 NCBIfam; TIGR01016; sucCoAbeta; 1. DR PANTHER; PTHR11815:SF1; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1. DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1. DR Pfam; PF08442; ATP-grasp_2; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001554; SucCS_beta; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 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 BINDING 100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT BINDING 107..109 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT BINDING 260 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT BINDING 274 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT BINDING 325 FT /ligand="substrate" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220" FT BINDING 382..384 FT /ligand="substrate" FT /ligand_note="ligand 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 //