SUCD_COXBU
ID SUCD_COXBU Reviewed; 294 AA.
AC P53591;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
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=CBU_1396;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nine Mile phase I;
RA Schimmels J.A., Mallavia L.P.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nine Mile phase I;
RA Thiele D., Willems H., Oswald W., Krauss H.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; U07789; AAA61788.1; -; Unassigned_DNA.
DR EMBL; X77919; CAA54877.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO90895.1; -; Genomic_DNA.
DR RefSeq; NP_820381.1; NC_002971.3.
DR RefSeq; WP_005771707.1; NZ_CCYB01000027.1.
DR AlphaFoldDB; P53591; -.
DR SMR; P53591; -.
DR STRING; 227377.CBU_1396; -.
DR DNASU; 1209302; -.
DR EnsemblBacteria; AAO90895; AAO90895; CBU_1396.
DR GeneID; 1209302; -.
DR KEGG; cbu:CBU_1396; -.
DR PATRIC; fig|227377.7.peg.1398; -.
DR eggNOG; COG0074; Bacteria.
DR HOGENOM; CLU_052104_0_0_6; -.
DR OMA; VIICITE; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..294
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha"
FT /id="PRO_0000102790"
FT ACT_SITE 248
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 160
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT CONFLICT 282..294
FT /note="GKGVAEATGWSTH -> AKALLRQQAGQLI (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> R (in Ref. 1; AAA61788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 30667 MW; 41602BD0D01493DE CRC64;
MSILIDKETR VLCQGFTGKQ GTFHSEQAIE YGTQMVGGVT PGKGGQSHLG LPIFNSVHEA
VEETSADATM IFVPAPFCKD SIIEAVDAGV RLVVCITEGI PVLDMLEVKA YLRQHPDVRM
IGPNCPGVIT PGECKIGIMP GHIHQRGKVG IVSRSGTLTY EAVNQTTQMG FGQSTCVGIG
GDPIPGTSFI DVLEMFEKDS QTQAIVMVGE IGGTAEEEAA EFIQSNVKKP VISYIAGVTA
PPGKRMGHAG AIIAGGKGTA ADKYAALEAA GVFVVKSPAE IGKGVAEATG WSTH
