SUCD_PSEAE
ID SUCD_PSEAE Reviewed; 295 AA.
AC Q51567; Q9X5W2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
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, ECO:0000269|PubMed:10671455};
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=PA1589;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10671455; DOI=10.1128/jb.182.5.1333-1339.2000;
RA Kapatral V., Bina X., Chakrabarty A.M.;
RT "Succinyl coenzyme A synthetase of Pseudomonas aeruginosa with a broad
RT specificity for nucleoside triphosphate (NTP) synthesis modulates
RT specificity for NTP synthesis by the 12-kilodalton form of nucleoside
RT diphosphate kinase.";
RL J. Bacteriol. 182:1333-1339(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8581173; DOI=10.1099/13500872-142-1-79;
RA Liao X., Charlebois I., Ouellet C., Morency M.J., Dewar K., Lightfoot J.,
RA Foster J., Siehnel R., Schweizer H., Lam J.S., Hancock R.E., Levesque R.C.;
RT "Physical mapping of 32 genetic markers on the Pseudomonas aeruginosa PAO1
RT chromosome.";
RL Microbiology 142:79-86(1996).
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. Can also
CC generate UTP or CTP, although it preferentially synthesizes ATP and/or
CC GTP. {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10671455}.
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, ECO:0000269|PubMed:10671455};
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; AF128399; AAD21623.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04978.1; -; Genomic_DNA.
DR EMBL; X84052; CAA58871.1; -; Genomic_DNA.
DR PIR; B83446; B83446.
DR RefSeq; NP_250280.1; NC_002516.2.
DR RefSeq; WP_003087428.1; NZ_QZGE01000003.1.
DR AlphaFoldDB; Q51567; -.
DR SMR; Q51567; -.
DR STRING; 287.DR97_300; -.
DR PaxDb; Q51567; -.
DR PRIDE; Q51567; -.
DR DNASU; 882039; -.
DR EnsemblBacteria; AAG04978; AAG04978; PA1589.
DR GeneID; 882039; -.
DR KEGG; pae:PA1589; -.
DR PATRIC; fig|208964.12.peg.1648; -.
DR PseudoCAP; PA1589; -.
DR HOGENOM; CLU_052104_0_0_6; -.
DR InParanoid; Q51567; -.
DR OMA; VIICITE; -.
DR PhylomeDB; Q51567; -.
DR BioCyc; PAER208964:G1FZ6-1619-MON; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042709; C:succinate-CoA ligase complex; IDA:PseudoCAP.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:PseudoCAP.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IDA:PseudoCAP.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:PseudoCAP.
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 1: Evidence at protein level;
KW Ligase; Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..295
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha"
FT /id="PRO_0000102797"
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"
FT CONFLICT 18..20
FT /note="GSQ -> VEP (in Ref. 3; CAA58871)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="L -> R (in Ref. 1; AAD21623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 30266 MW; D1BE36033FEA716F CRC64;
MSVLINKDTK VICQGFTGSQ GTFHSEQAIA YGTKMVGGVT PGKGGTTHLG LPVFNTVKEA
VEATGAEASV IYVPAPFCKD SILEAAFGGI KLIVCITEGI PTLDMLDAKV KCDELGVRLI
GPNCPGVITP GECKIGIMPG HIHLPGKVGI VSRSGTLTYE AVKQTTDAGF GQSTCVGIGG
DPIPGSNFID ILKLFQEDPQ TEAIVMIGEI GGSAEEEAAA FIKANVTKPV VSYIAGVTAP
PGKRMGHAGA IISGGKGTAD EKFAALQDAG VKTVRSLADI GKALAELTGW EVKKA
