SUCB1_MOUSE
ID SUCB1_MOUSE Reviewed; 463 AA.
AC Q9Z2I9; Q3TVH1; Q8BGS6;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03220};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03220};
DE AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03220};
DE Short=A-SCS {ECO:0000255|HAMAP-Rule:MF_03220};
DE AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000255|HAMAP-Rule:MF_03220};
DE Short=SCS-betaA {ECO:0000255|HAMAP-Rule:MF_03220};
DE Flags: Precursor;
GN Name=Sucla2 {ECO:0000255|HAMAP-Rule:MF_03220};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Head, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-463.
RC TISSUE=Heart;
RX PubMed=9765291; DOI=10.1074/jbc.273.42.27580;
RA Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.;
RT "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA
RT synthetases in multicellular eucaryotes.";
RL J. Biol. Chem. 273:27580-27586(1998).
RN [4]
RP PROTEIN SEQUENCE OF 121-129; 206-215; 337-362 AND 443-451, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND THR-341, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-88; LYS-129; LYS-139;
RP LYS-216; LYS-368 AND LYS-438, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_03220};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03220};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03220};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03220}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC determines specificity for ATP. Interacts with ALAS2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9P2R7, ECO:0000255|HAMAP-Rule:MF_03220}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03220}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. ATP-specific subunit beta subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03220}.
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DR EMBL; AK081965; BAC38380.1; -; mRNA.
DR EMBL; AK088801; BAC40580.1; -; mRNA.
DR EMBL; AK132762; BAE21343.1; -; mRNA.
DR EMBL; AK160130; BAE35647.1; -; mRNA.
DR EMBL; AK160652; BAE35942.1; -; mRNA.
DR EMBL; BC056353; AAH56353.1; -; mRNA.
DR EMBL; BC057605; AAH57605.1; -; mRNA.
DR EMBL; AF058955; AAC64398.1; -; mRNA.
DR CCDS; CCDS27271.1; -.
DR RefSeq; NP_035636.1; NM_011506.3.
DR AlphaFoldDB; Q9Z2I9; -.
DR SMR; Q9Z2I9; -.
DR BioGRID; 203570; 55.
DR CORUM; Q9Z2I9; -.
DR IntAct; Q9Z2I9; 9.
DR STRING; 10090.ENSMUSP00000123765; -.
DR iPTMnet; Q9Z2I9; -.
DR PhosphoSitePlus; Q9Z2I9; -.
DR SwissPalm; Q9Z2I9; -.
DR REPRODUCTION-2DPAGE; IPI00261627; -.
DR REPRODUCTION-2DPAGE; Q9Z2I9; -.
DR UCD-2DPAGE; Q9Z2I9; -.
DR EPD; Q9Z2I9; -.
DR jPOST; Q9Z2I9; -.
DR MaxQB; Q9Z2I9; -.
DR PaxDb; Q9Z2I9; -.
DR PeptideAtlas; Q9Z2I9; -.
DR PRIDE; Q9Z2I9; -.
DR ProteomicsDB; 258670; -.
DR Antibodypedia; 23774; 135 antibodies from 27 providers.
DR DNASU; 20916; -.
DR Ensembl; ENSMUST00000022706; ENSMUSP00000022706; ENSMUSG00000022110.
DR Ensembl; ENSMUST00000160507; ENSMUSP00000123765; ENSMUSG00000022110.
DR GeneID; 20916; -.
DR KEGG; mmu:20916; -.
DR UCSC; uc007upx.1; mouse.
DR CTD; 8803; -.
DR MGI; MGI:1306775; Sucla2.
DR VEuPathDB; HostDB:ENSMUSG00000022110; -.
DR eggNOG; KOG2799; Eukaryota.
DR GeneTree; ENSGT00390000010170; -.
DR HOGENOM; CLU_037430_0_0_1; -.
DR InParanoid; Q9Z2I9; -.
DR OMA; ITACDEV; -.
DR OrthoDB; 973871at2759; -.
DR PhylomeDB; Q9Z2I9; -.
DR TreeFam; TF300624; -.
DR BRENDA; 6.2.1.5; 3474.
DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00999.
DR BioGRID-ORCS; 20916; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Sucla2; mouse.
DR PRO; PR:Q9Z2I9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9Z2I9; protein.
DR Bgee; ENSMUSG00000022110; Expressed in atrioventricular valve and 265 other tissues.
DR Genevisible; Q9Z2I9; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0004774; F:succinate-CoA ligase activity; ISS:MGI.
DR GO; GO:0006105; P:succinate metabolic process; ISO:MGI.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISO:MGI.
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 Acetylation; ATP-binding; Direct protein sequencing; Ligase; Magnesium;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT CHAIN 54..463
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT /id="PRO_0000033353"
FT DOMAIN 61..288
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 105..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 323
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 380..382
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 94
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 162
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 84
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 438
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 463 AA; 50114 MW; 74CE8E962BC0BB27 CRC64;
MAASMFYGRQ LAAAALRSHR PQTTLRAAAQ VLGNSGLFNK HGLQVQQQQQ RTLSLHEYLS
MELLQEAGVS VPKGFVAKSS DEAYAIAKKL GSKDVVIKAQ VLAGGRGKGT FTSGLKGGVK
IVFSPEEAKA VSSQMIGQKL ITKQTGEKGR ICNQVLVCER KYPRREYYFA ITMERSFQGP
VLIGSAQGGV NIEDVAAENP EAIVKEPIDI VEGIKKEQAV TLAQKMGFPS NIVDSAAENM
IKLYNLFLKY DATMVEINPM VEDSDGKVLC MDAKINFDSN SAYRQKKIFD LQDWSQEDER
DKEAANADIN YIGLDGSIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG GATVQQVTEA
FKLITSDKKV QAILVNIFGG IMRCDVIAQG IVMAVKDLEI RIPVVVRLQG TRVDDAKALI
ADSGLKILAC DDLDEAAKMV VKLSEIVTLA KEAHVDVKFQ LPI
