ID Q9PL98_CHLMU Unreviewed; 291 AA.
AC Q9PL98;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 146.
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:AAF39081.1};
GN OrderedLocusNames=TC_0209 {ECO:0000313|EMBL:AAF39081.1};
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161 {ECO:0000313|EMBL:AAF39081.1, ECO:0000313|Proteomes:UP000000800};
RN [1] {ECO:0000313|EMBL:AAF39081.1, ECO:0000313|Proteomes:UP000000800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg {ECO:0000313|Proteomes:UP000000800};
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE002160; AAF39081.1; -; Genomic_DNA.
DR PIR; H81729; H81729.
DR RefSeq; WP_010229825.1; NZ_CP063055.1.
DR AlphaFoldDB; Q9PL98; -.
DR GeneID; 1246335; -.
DR KEGG; cmu:TC_0209; -.
DR PATRIC; fig|243161.6.peg.228; -.
DR eggNOG; COG0074; Bacteria.
DR HOGENOM; CLU_052104_0_0_0; -.
DR OrthoDB; 9807196at2; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000000800; 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..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 291 AA; 30262 MW; B6494ABE03FD2F59 CRC64;
MLELLNKDLP IITQGITGKA GSFHTTQCVA YGSNFVGGVT PGKGGTQFLD LPIFDSVLEA
KQATGCRASM IFVPPPFAAE AIFEAEDAGI ELIVCITEGI PVQDMLAVNS LMEKSSCRLV
GPNCPGVIKP GACKIGIMPG YIHLPGNVGV ISRSGTLTYE AVWQLTQRKI GQSVCIGIGG
DPLNGTSFID VLQELEKDEQ TEAILMIGEI GGSAEEDAAD WISQHCSKPV IAFIAGATAP
KGKRMGHAGA IISGNSGDAF SKQRALREAG VVVVESPALI GEAVASVLNS H
//
