ID A9IKE6_BORPD Unreviewed; 293 AA.
AC A9IKE6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 102.
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:CAP42402.1};
GN OrderedLocusNames=Bpet2062 {ECO:0000313|EMBL:CAP42402.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42402.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP42402.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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; AM902716; CAP42402.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IKE6; -.
DR STRING; 94624.Bpet2062; -.
DR KEGG; bpt:Bpet2062; -.
DR eggNOG; COG0074; Bacteria.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000001225; Chromosome.
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; 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..103
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 252
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 46
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT BINDING 99..101
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT BINDING 164
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
SQ SEQUENCE 293 AA; 30728 MW; CB02101BA0BEE488 CRC64;
MSILINKDTK VITQGITGKT GQFHTRMCRE YANGKAAFVA GVHPKKAGED FEGVPIFGSV
QDAKDKTGAT VSVIYVPPAG AAAAIWEAVE AELDLVICIT EGIPVRDMLE VKNRMKAKNS
KTLLLGPNCP GLITPDEIKI GIMPGHIHRK GRIGIVSRSG TLTYEAVAQV TELGLGQSSA
VGIGGDPING LKHVDVLKLF NDDPDTDAVI MIGEIGGPDE VNAAQWAKDN MKKPVVGFIA
GVTAPPGKRM GHAGALISGG ADTADAKLEV MEACGIRTTR NPSEMGKLLK SVL
//
