ID A0A291JKD4_9STAP Unreviewed; 302 AA.
AC A0A291JKD4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ECO:0000313|EMBL:RIO43160.1};
GN ORFNames=BJD96_08420 {ECO:0000313|EMBL:ATH60324.1}, BUZ60_05690
GN {ECO:0000313|EMBL:RIO43160.1}, BUZ61_03380
GN {ECO:0000313|EMBL:PTK60092.1}, CD130_08630
GN {ECO:0000313|EMBL:PNZ97312.1}, NCTC13834_01694
GN {ECO:0000313|EMBL:SUM55331.1};
OS Staphylococcus nepalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=214473 {ECO:0000313|EMBL:ATH60324.1, ECO:0000313|Proteomes:UP000217956};
RN [1] {ECO:0000313|Proteomes:UP000240400, ECO:0000313|Proteomes:UP000265695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 4025 {ECO:0000313|EMBL:RIO43160.1,
RC ECO:0000313|Proteomes:UP000265695}, and SNUC 4337
RC {ECO:0000313|EMBL:PTK60092.1, ECO:0000313|Proteomes:UP000240400};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
RN [2] {ECO:0000313|EMBL:ATH60324.1, ECO:0000313|Proteomes:UP000217956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1 {ECO:0000313|EMBL:ATH60324.1,
RC ECO:0000313|Proteomes:UP000217956};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Staphylococcus nepalensis JS1.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PNZ97312.1, ECO:0000313|Proteomes:UP000236280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15150 {ECO:0000313|EMBL:PNZ97312.1,
RC ECO:0000313|Proteomes:UP000236280};
RA Cole K., Golubchik T., Russell J., Foster D., Llewelyn M., Wilson D.,
RA Crook D., Paul J.;
RT "Draft genome sequences of 64 type strains of genus Staph aureus.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PTK60092.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SNUC 4337 {ECO:0000313|EMBL:PTK60092.1};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:SUM55331.1, ECO:0000313|Proteomes:UP000254412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13834 {ECO:0000313|EMBL:SUM55331.1,
RC ECO:0000313|Proteomes:UP000254412};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:RIO43160.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SNUC 4025 {ECO:0000313|EMBL:RIO43160.1};
RA Parvin R., Begum J.A., Chowdhury E.H., Islam M.R., Harder T.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU000699}.
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, ECO:0000256|RuleBase:RU000699};
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, ECO:0000256|RuleBase:RU000699}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000256|HAMAP-Rule:MF_01988,
CC ECO:0000256|RuleBase:RU000677}.
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DR EMBL; CP017460; ATH60324.1; -; Genomic_DNA.
DR EMBL; PPRR01000140; PNZ97312.1; -; Genomic_DNA.
DR EMBL; PZHR01000010; PTK60092.1; -; Genomic_DNA.
DR EMBL; QXVN01000017; RIO43160.1; -; Genomic_DNA.
DR EMBL; UHDS01000001; SUM55331.1; -; Genomic_DNA.
DR KEGG; snl:BJD96_08420; -.
DR OrthoDB; 9807196at2; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000217956; Chromosome.
DR Proteomes; UP000236280; Unassembled WGS sequence.
DR Proteomes; UP000240400; Unassembled WGS sequence.
DR Proteomes; UP000254412; Unassembled WGS sequence.
DR Proteomes; UP000265695; 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: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; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
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.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000677};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01988};
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 247
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988,
FT ECO:0000256|PIRSR:PIRSR001553-1"
FT BINDING 17..20
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
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 159
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
SQ SEQUENCE 302 AA; 31751 MW; EB8BDED613D9730E CRC64;
MSVMIDKNTK VIVQGITGST ALFHTKQMLE YGTQIVAGVT PGKGGQVVEG VPVFNTVEEA
KQETGATVSV IYVPAPFAAD AILECIEAEL DLAICITEHI PVIDMVKVKR YSEGKKTRVI
GPNCPGVITA DECKIGIMPG YIHKKGHVGV VSRSGTLTYE AVHQLTEEGI GQTTAVGIGG
DPVNGTNFID VLKQFNEDDE TKAVVMIGEI GGTAEEEAAE WIKDNMDKPV VGFVGGQTAP
PGKRMGHAGA IVSGGKGTAE EKIKTLNSCG VKTADTPSEI GTTLIEAAKE VGIYEQLLTV
KQ
//
