SUCB2_CAEEL
ID SUCB2_CAEEL Reviewed; 415 AA.
AC P53589;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000250|UniProtKB:Q96I99, 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=sucg-1 {ECO:0000312|WormBase:C50F7.4};
GN ORFNames=C50F7.4 {ECO:0000312|WormBase:C50F7.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- 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; FO080878; CCD67452.1; -; Genomic_DNA.
DR PIR; T29296; T29296.
DR RefSeq; NP_501266.1; NM_068865.4.
DR AlphaFoldDB; P53589; -.
DR SMR; P53589; -.
DR BioGRID; 42673; 3.
DR STRING; 6239.C50F7.4; -.
DR EPD; P53589; -.
DR PaxDb; P53589; -.
DR PeptideAtlas; P53589; -.
DR EnsemblMetazoa; C50F7.4.1; C50F7.4.1; WBGene00016844.
DR GeneID; 177555; -.
DR KEGG; cel:CELE_C50F7.4; -.
DR UCSC; C50F7.4; c. elegans.
DR CTD; 177555; -.
DR WormBase; C50F7.4; CE04242; WBGene00016844; sucg-1.
DR eggNOG; KOG1447; Eukaryota.
DR GeneTree; ENSGT00390000010170; -.
DR HOGENOM; CLU_037430_0_0_1; -.
DR InParanoid; P53589; -.
DR OMA; AIQQFKV; -.
DR OrthoDB; 973871at2759; -.
DR PhylomeDB; P53589; -.
DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00999.
DR PRO; PR:P53589; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00016844; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
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: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; 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; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 3: Inferred from homology;
KW GTP-binding; Ligase; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT CHAIN 20..415
FT /note="Succinate--CoA ligase [GDP-forming] subunit beta,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT /id="PRO_0000033359"
FT DOMAIN 28..258
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 72..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 292
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 349..351
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT SITE 61
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT SITE 131
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
SQ SEQUENCE 415 AA; 45092 MW; A6B234E2A951E6E7 CRC64;
MLRAAGNLSK SMMKSQRRFL NLQEFQSKEI LEKHGCSVQN FVVASNRKEA EEKWMSFGDH
EYVVKAQILA GGRGKGKFIN GTKGIGGVFI TKEKDAALEA IDEMIGKRLV TKQTTSEGVR
VDKVMIAEGV DIKRETYLAV LMDRESNGPV VVASPDGGMD IEAVAEKTPE RIFKTPIDIQ
MGMTEGQSLK IAKDLQFEGK LIGVAAQEIK RLYDLFIAVD ATQVEINPLV ETADGRVFCV
DAKMNFDDSA AYRQKEIFAY ETFEEHDPRE VDAHQFNLNY IGMDGNIACL VNGAGLAMAT
MDLIKLHGGE PANFLDVGGA VTEDAVFNAV RIITSDPRVK CVLINIFGGI VNCATIANGV
VSAVNKIGLN VPMVVRLEGT NVDAAKQIMK KSGLKILTAN NLDEAAAKAV SSLPK
