ID   F1LM47_RAT              Unreviewed;       465 AA.
AC   F1LM47;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   02-JUN-2021, entry version 68.
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.
CC       {ECO:0000256|RuleBase:RU361258}.
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. {ECO:0000256|RuleBase:RU361258}.
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}.
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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
//