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SUCD_MYCBO
ID   SUCD_MYCBO              Reviewed;         303 AA.
AC   Q7U0Z0; A0A1R3XX97; X2BGN0;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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};
GN   OrderedLocusNames=BQ2027_MB0977;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT99575.1; -; Genomic_DNA.
DR   RefSeq; NP_854634.1; NC_002945.3.
DR   RefSeq; WP_003903242.1; NC_002945.4.
DR   AlphaFoldDB; Q7U0Z0; -.
DR   SMR; Q7U0Z0; -.
DR   EnsemblBacteria; SIT99575; SIT99575; BQ2027_MB0977.
DR   PATRIC; fig|233413.5.peg.1064; -.
DR   OMA; VIICITE; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001419; 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..303
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit alpha"
FT                   /id="PRO_0000102795"
FT   ACT_SITE        259
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         20..23
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         46
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         108..110
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
SQ   SEQUENCE   303 AA;  31201 MW;  7134F8C3D9FBC3C1 CRC64;
     MTHMSIFLSR DNKVIVQGIT GSEATVHTAR MLRAGTQIVG GVNARKAGTT VTHEDKGGRL
     IKLPVFGSVA EAMEKTGADV SIIFVPPTFA KDAIIEAIDA EIPLLVVITE GIPVQDTAYA
     WAYNLEAGHK TRIIGPNCPG IISPGQSLAG ITPANITGPG PIGLVSKSGT LTYQMMFELR
     DLGFSTAIGI GGDPVIGTTH IDAIEAFEKD PDTKLIVMIG EIGGDAEERA ADFIKTNVSK
     PVVGYVAGFT APEGKTMGHA GAIVSGSSGT AAAKQEALEA AGVKVGKTPS ATAALAREIL
     LSL
 
 
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