SUCD_ECOL6
ID SUCD_ECOL6 Reviewed; 289 AA.
AC P0AGF0; P07459;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha {ECO:0000255|HAMAP-Rule:MF_01988};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_01988};
DE AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01988};
DE Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_01988};
GN Name=sucD {ECO:0000255|HAMAP-Rule:MF_01988}; OrderedLocusNames=c0806;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01988};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01988}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01988}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01988}.
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DR EMBL; AE014075; AAN79279.1; -; Genomic_DNA.
DR RefSeq; WP_000025458.1; NC_004431.1.
DR AlphaFoldDB; P0AGF0; -.
DR SMR; P0AGF0; -.
DR STRING; 199310.c0806; -.
DR PRIDE; P0AGF0; -.
DR EnsemblBacteria; AAN79279; AAN79279; c0806.
DR GeneID; 67413769; -.
DR KEGG; ecc:c0806; -.
DR eggNOG; COG0074; Bacteria.
DR HOGENOM; CLU_052104_0_0_6; -.
DR OMA; VIICITE; -.
DR BioCyc; ECOL199310:C0806-MON; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000001410; 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.261; -; 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; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001553; SucCS_alpha; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 3: Inferred from homology;
KW Ligase; Nucleotide-binding; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..289
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha"
FT /id="PRO_0000102793"
FT ACT_SITE 247
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 17..20
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 43
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 96..98
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 159
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
SQ SEQUENCE 289 AA; 29777 MW; 8AC27AD828BC51B3 CRC64;
MSILIDKNTK VICQGFTGSQ GTFHSEQAIA YGTKMVGGVT PGKGGTTHLG LPVFNTVREA
VAATGATASV IYVPAPFCKD SILEAIDAGI KLIITITEGI PTLDMLTVKV KLDEAGVRMI
GPNCPGVITP GECKIGIQPG HIHKPGKVGI VSRSGTLTYE AVKQTTDYGF GQSTCVGIGG
DPIPGSNFID ILEMFEKDPQ TEAIVMIGEI GGSAEEEAAA YIKEHVTKPV VGYIAGVTAP
KGKRMGHAGA IIAGGKGTAD EKFAALEAAG VKTVRSLADI GEALKTVLK
