SUCB1_CAEEL
ID SUCB1_CAEEL Reviewed; 435 AA.
AC P53588;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03220};
DE EC=6.2.1.5 {ECO:0000250|UniProtKB:Q9YI37, 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=suca-1 {ECO:0000312|WormBase:F47B10.1};
GN ORFNames=F47B10.1 {ECO:0000312|WormBase:F47B10.1};
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: 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. {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; Z68004; CAA91981.1; -; Genomic_DNA.
DR PIR; T22332; T22332.
DR RefSeq; NP_509821.1; NM_077420.3.
DR AlphaFoldDB; P53588; -.
DR SMR; P53588; -.
DR BioGRID; 46191; 11.
DR DIP; DIP-26345N; -.
DR IntAct; P53588; 2.
DR STRING; 6239.F47B10.1; -.
DR EPD; P53588; -.
DR PaxDb; P53588; -.
DR PeptideAtlas; P53588; -.
DR EnsemblMetazoa; F47B10.1.1; F47B10.1.1; WBGene00009812.
DR GeneID; 181280; -.
DR KEGG; cel:CELE_F47B10.1; -.
DR UCSC; F47B10.1.1; c. elegans.
DR CTD; 181280; -.
DR WormBase; F47B10.1; CE03351; WBGene00009812; suca-1.
DR eggNOG; KOG2799; Eukaryota.
DR GeneTree; ENSGT00390000010170; -.
DR HOGENOM; CLU_037430_0_0_1; -.
DR InParanoid; P53588; -.
DR OMA; ITACDEV; -.
DR OrthoDB; 973871at2759; -.
DR PhylomeDB; P53588; -.
DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00999.
DR PRO; PR:P53588; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00009812; Expressed in embryo and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
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; 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_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 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT CHAIN 21..435
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT /id="PRO_0000033355"
FT DOMAIN 32..259
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 76..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 294
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 352..354
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 65
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 133
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
SQ SEQUENCE 435 AA; 47419 MW; E91C4BD4CF82F7CB CRC64;
MIGRISQPLL NTSQKFMAPA ARTLMLHEHH GMKILQNYEI KVPPFGVAQD AETAFSEAKR
IGGKDYVVKA QVLAGGRGKG RFSSGLQGGV QIVFTPDEVK QKAGMMIGAN LITKQTDHRG
KKCEEVMVCK RLFTRREYYF SITLDRNTNG PIVIASSQGG VNIEEVAATN PDAIVKMPID
VNVGITKELA HEIAVKMGFS KDCEQQASEI IEKLYQMFKG SDATLVEINP MAEDVNGDVY
CMDCKLLLDS NAEFRQAKLF DLKDKKQEDE LEIRAAAANL NYIRLDGTIG CMVNGAGLAM
ATMDIIKLHG GEPANFLDVG GGATVEQVTE AFKIITADKD KVSAILVNIF GGIMRCDVIA
QGIIQAAREL DLKIPIVVRL QGTKVEDAKA LIATSQLRIL PCDNLDEAAK MVVKLSNIVD
LARATNVDVK FELSI
