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-FEB-2019, entry version 58.
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}.
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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   UniGene; Rn.62159; -.
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; LCMDAKF; -.
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: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
//