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TRPC_BRUME
ID   TRPC_BRUME              Reviewed;         268 AA.
AC   P66988; Q8G0F4; Q8YHF8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00134};
DE            Short=IGPS {ECO:0000255|HAMAP-Rule:MF_00134};
DE            EC=4.1.1.48 {ECO:0000255|HAMAP-Rule:MF_00134};
GN   Name=trpC {ECO:0000255|HAMAP-Rule:MF_00134}; OrderedLocusNames=BMEI0843;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00134};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00134}.
CC   -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00134}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL52024.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL52024.1; ALT_INIT; Genomic_DNA.
DR   PIR; AE3357; AE3357.
DR   RefSeq; WP_002964269.1; NZ_CP007763.1.
DR   AlphaFoldDB; P66988; -.
DR   SMR; P66988; -.
DR   STRING; 224914.BMEI0843; -.
DR   EnsemblBacteria; AAL52024; AAL52024; BMEI0843.
DR   GeneID; 45052184; -.
DR   GeneID; 55590824; -.
DR   KEGG; bme:BMEI0843; -.
DR   KEGG; bmel:DK63_577; -.
DR   PATRIC; fig|224914.52.peg.601; -.
DR   eggNOG; COG0134; Bacteria.
DR   OMA; RGPHDLI; -.
DR   PhylomeDB; P66988; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000419; Chromosome I.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00331; IGPS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00134_B; IGPS_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854; PTHR22854; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   PROSITE; PS00614; IGPS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Lyase; Tryptophan biosynthesis.
FT   CHAIN           1..268
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_0000154216"
SQ   SEQUENCE   268 AA;  29269 MW;  7BDF1668C6EAEC55 CRC64;
     MSTDILRKIE AYKREEIAAA KARLALDELK ARTRDQSAPR GFLKALEAKR AAGQFALIAE
     IKKASPSKGL IRPDFDPPAL AKAYEEGGAA CLSVLTDTPS FQGAPEFLTA ARQACSLPAL
     RKDFLFDPYQ VYEARSWGAD CILIIMASVD DDLAKELEDT AFALGMDALI EVHDEAEMER
     ALKLSSRLLG VNNRNLRSFE VNLAVSERLA KMAPSDRLLV GESGIFTHED CLRLEKSGIG
     TFLIGESLMR QHDVAAATRA LLTGAEKL
 
 
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