ID V7EMD9_9RHOB Unreviewed; 299 AA.
AC V7EMD9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha {ECO:0000256|HAMAP-Rule:MF_01988};
DE EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_01988};
DE AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01988};
DE Short=SCS-alpha {ECO:0000256|HAMAP-Rule:MF_01988};
GN Name=sucD {ECO:0000256|HAMAP-Rule:MF_01988};
GN ORFNames=Q27BPR15_07110 {ECO:0000313|EMBL:ESW61337.1};
OS Rhodobacter sp. CACIA14H1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1408890 {ECO:0000313|EMBL:ESW61337.1, ECO:0000313|Proteomes:UP000018503};
RN [1] {ECO:0000313|EMBL:ESW61337.1, ECO:0000313|Proteomes:UP000018503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24435858;
RA Lima A.R., Siqueira A.S., Dos Santos B.G., da Silva F.D., Inada D.T.,
RA Lima C.P., Cardoso J.F., Vianez-Junior J.L., Nunes M.R., Goncalves E.C.;
RT "Draft Genome Sequence of Rhodobacter sp. Strain CACIA 14H1, a
RT Heterotrophic Bacterium Obtained from a Nonaxenic Culture of a Cyanobium
RT Species.";
RL Genome Announc. 2:e01116-13(2014).
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC either ATP or GTP and thus represents the only step of substrate-level
CC phosphorylation in the TCA. The alpha subunit of the enzyme binds the
CC substrates coenzyme A and phosphate, while succinate binding and
CC nucleotide specificity is provided by the beta subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01988}.
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_01988};
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; Evidence={ECO:0000256|HAMAP-Rule:MF_01988};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01988}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_01988}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000256|HAMAP-Rule:MF_01988}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01988}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESW61337.1}.
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DR EMBL; AYNO01000036; ESW61337.1; -; Genomic_DNA.
DR AlphaFoldDB; V7EMD9; -.
DR STRING; 1408890.Q27BPR15_07110; -.
DR PATRIC; fig|449393.3.peg.1444; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000018503; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; IEA:RHEA.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005810; CoA_lig_alpha.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01019; sucCoAalpha; 1.
DR PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001553; SucCS_alpha; 1.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000313|EMBL:ESW61337.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01988};
KW Reference proteome {ECO:0000313|Proteomes:UP000018503};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_01988}.
FT DOMAIN 4..100
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 251
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988,
FT ECO:0000256|PIRSR:PIRSR001553-1"
FT BINDING 43
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT BINDING 96..98
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT BINDING 163
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
SQ SEQUENCE 299 AA; 30998 MW; 99CAB9D884C80548 CRC64;
MAILITEKTR VIVQGMSGRI GQFHAQDMIK HGTNVVGGVT PGKGGESLLG RPLFNTVREA
VEATGAEASL VFVPPPFAAD AIMEAADAGI KTAVCVTDGI PAQDMMKVKR FLKRYPAERK
MRLIGPNCAG IISPGKGFMG IMPPHIYMPG RVGIVGRSGT LGYEAASQMK ALGIGVSTSV
GIGGDPINGS SFRDILELFE ADPETDAVMM IGEIGGPQEA EAALYARNFM KKPVVAYIAG
LSAPKGRKMG HAGAIISAFG ESAQEKVEIL SAAGITIAPN PSAMGETMAS VLASRRAAA
//
