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SUCD_RICBR
ID   SUCD_RICBR              Reviewed;         291 AA.
AC   Q1RH56;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=RBE_1227;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05308.1; -; Genomic_DNA.
DR   RefSeq; WP_011477883.1; NC_007940.1.
DR   AlphaFoldDB; Q1RH56; -.
DR   SMR; Q1RH56; -.
DR   STRING; 336407.RBE_1227; -.
DR   PRIDE; Q1RH56; -.
DR   EnsemblBacteria; ABE05308; ABE05308; RBE_1227.
DR   KEGG; rbe:RBE_1227; -.
DR   eggNOG; COG0074; Bacteria.
DR   HOGENOM; CLU_052104_0_0_5; -.
DR   OMA; VIICITE; -.
DR   OrthoDB; 1081709at2; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001951; 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   CHAIN           1..291
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit alpha"
FT                   /id="PRO_0000286487"
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         159
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
SQ   SEQUENCE   291 AA;  30099 MW;  DAE3C21650BE9400 CRC64;
     MAILVNKKTK VICQGFTGSQ GTFHSEQAIA YGTKMVGGVT PGKGGKTHLD LPIYNTVHEA
     KAKTGANASV IYVPPPFAAD SILEAIDAGI EIVVCITEGI PVLDMVRVKR ALVGSRTRLI
     GPNCPGIITP DECKIGIMPG HIHRKGSIGI VSRSGTLTYE AVAQTTAVGL GQSTCVGIGG
     DPVNGTNFVD CIDMFLQDDE TKAIIMIGEI GGDAEENAAD FIKHSKIKKP IVSFIAGITA
     PPGKRMGHAG AIIAGGKGSA EDKLEALQSA GVTITRSPAD IGKTMLDLLN G
 
 
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