SUCB2_MOUSE
ID SUCB2_MOUSE Reviewed; 433 AA.
AC Q9Z2I8; Q3T9B8; Q3TJQ5; Q3TK63; Q66JT3; Q7TMY3; Q80VV1; Q8K2K9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221};
DE EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03221};
DE AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=G-SCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=GTPSCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE AltName: Full=Succinyl-CoA synthetase beta-G chain {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=SCS-betaG {ECO:0000255|HAMAP-Rule:MF_03221};
DE Flags: Precursor;
GN Name=Suclg2 {ECO:0000255|HAMAP-Rule:MF_03221};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Placenta, and Spleen;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Kidney, Liver, and Mammary tumor;
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 30-433 (ISOFORM 1).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-217, 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 [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-67; LYS-79 AND LYS-339, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67; LYS-74; LYS-112; LYS-133;
RP LYS-140; LYS-201; LYS-219; LYS-228; LYS-272; LYS-348; LYS-387; LYS-407 AND
RP LYS-424, AND IDENTIFICATION BY MASS SPECTROMETRY [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: GTP-specific succinyl-CoA synthetase functions in the citric
CC acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC synthesis of GTP 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_03221}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03221};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03221};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03221};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03221}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC determines specificity for GTP. {ECO:0000255|HAMAP-Rule:MF_03221}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03221}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z2I8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2I8-2; Sequence=VSP_016905;
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. GTP-specific subunit beta subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03221}.
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DR EMBL; AK167136; BAE39282.1; -; mRNA.
DR EMBL; AK167339; BAE39440.1; -; mRNA.
DR EMBL; AK172561; BAE43068.1; -; mRNA.
DR EMBL; AK172633; BAE43106.1; -; mRNA.
DR EMBL; BC030947; AAH30947.1; -; mRNA.
DR EMBL; BC043312; AAH43312.1; -; mRNA.
DR EMBL; BC054425; AAH54425.1; -; mRNA.
DR EMBL; BC080781; AAH80781.1; -; mRNA.
DR EMBL; AF058956; AAC64399.1; -; mRNA.
DR CCDS; CCDS20381.1; -. [Q9Z2I8-1]
DR CCDS; CCDS85100.1; -. [Q9Z2I8-2]
DR RefSeq; NP_001313487.1; NM_001326558.1. [Q9Z2I8-2]
DR RefSeq; NP_035637.2; NM_011507.3. [Q9Z2I8-1]
DR AlphaFoldDB; Q9Z2I8; -.
DR SMR; Q9Z2I8; -.
DR BioGRID; 203571; 13.
DR CORUM; Q9Z2I8; -.
DR IntAct; Q9Z2I8; 5.
DR MINT; Q9Z2I8; -.
DR STRING; 10090.ENSMUSP00000078774; -.
DR iPTMnet; Q9Z2I8; -.
DR PhosphoSitePlus; Q9Z2I8; -.
DR SwissPalm; Q9Z2I8; -.
DR REPRODUCTION-2DPAGE; Q9Z2I8; -.
DR EPD; Q9Z2I8; -.
DR jPOST; Q9Z2I8; -.
DR MaxQB; Q9Z2I8; -.
DR PaxDb; Q9Z2I8; -.
DR PeptideAtlas; Q9Z2I8; -.
DR PRIDE; Q9Z2I8; -.
DR ProteomicsDB; 257474; -. [Q9Z2I8-1]
DR ProteomicsDB; 257475; -. [Q9Z2I8-2]
DR Antibodypedia; 31838; 129 antibodies from 26 providers.
DR DNASU; 20917; -.
DR Ensembl; ENSMUST00000079847; ENSMUSP00000078774; ENSMUSG00000061838. [Q9Z2I8-2]
DR Ensembl; ENSMUST00000204224; ENSMUSP00000144827; ENSMUSG00000061838. [Q9Z2I8-1]
DR GeneID; 20917; -.
DR KEGG; mmu:20917; -.
DR UCSC; uc009daa.3; mouse. [Q9Z2I8-1]
DR CTD; 8801; -.
DR MGI; MGI:1306824; Suclg2.
DR VEuPathDB; HostDB:ENSMUSG00000061838; -.
DR eggNOG; KOG1447; Eukaryota.
DR GeneTree; ENSGT00390000010170; -.
DR HOGENOM; CLU_037430_0_1_1; -.
DR InParanoid; Q9Z2I8; -.
DR OMA; AIQQFKV; -.
DR OrthoDB; 973871at2759; -.
DR PhylomeDB; Q9Z2I8; -.
DR TreeFam; TF300624; -.
DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00999.
DR BioGRID-ORCS; 20917; 0 hits in 78 CRISPR screens.
DR ChiTaRS; Suclg2; mouse.
DR PRO; PR:Q9Z2I8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z2I8; protein.
DR Bgee; ENSMUSG00000061838; Expressed in right kidney and 134 other tissues.
DR ExpressionAtlas; Q9Z2I8; baseline and differential.
DR Genevisible; Q9Z2I8; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
DR GO; GO:0045244; C:succinate-CoA ligase complex (GDP-forming); ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP 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; IEA:UniProtKB-UniRule.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; ISA:MGI.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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_03221; Succ_CoA_betaG_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; IPR034722; Succ_CoA_betaG_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; Alternative splicing; GTP-binding; Ligase; Magnesium;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q96I99"
FT CHAIN 39..433
FT /note="Succinate--CoA ligase [GDP-forming] subunit beta,
FT mitochondrial"
FT /id="PRO_0000033357"
FT DOMAIN 47..275
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 91..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 309
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 366..368
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT SITE 80
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT SITE 148
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT MOD_RES 67
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 67
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 79
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 133
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 339
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 348
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 387
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 407
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 424
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016905"
FT CONFLICT 66
FT /note="A -> T (in Ref. 1; BAE43106/BAE43068)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="I -> L (in Ref. 3; AAC64399)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..176
FT /note="GV -> RS (in Ref. 3; AAC64399)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="L -> P (in Ref. 2; AAH80781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 46840 MW; 8CA9C7998D2F2957 CRC64;
MASPVAIAAQ AGKLLRERAL RPLLAVRSQA GHLTPRRWLN LQEYQSKKLM SEHGVRVQRF
FVANTAKEAL EAAKRLNAKE IVLKAQILAG GRGKGVFNSG LKGGVHLTKD PKVVGELAQQ
MIGYNLATKQ TPKEGVKVNK VMVAEALDIS RETYLAILMD RSHNGPVIVG SPQGGVDIEE
VAASSPELIF KEQIDIFEGI KDSQAQRMAE NLGFLGSLKN QAADQITKLY HLFLKIDATQ
VEVNPFGETP EGQVVCFDAK INFDDNAEFR QKDIFAMDDK SENEPIENEA ARYDLKYIGL
DGNIACFVNG AGLAMATCDI IFLNGGKPAN FLDLGGGVKE AQVYEAFKLL TSDPKVEAIL
VNIFGGIVNC AIIANGITKA CRELELKVPL VVRLEGTNVQ EAQNILKSSG LPITSAVDLE
DAAKKAVASV AKK
