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T23O_CAUVC
ID   T23O_CAUVC              Reviewed;         263 AA.
AC   Q9A4E8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE            Short=TDO {ECO:0000255|HAMAP-Rule:MF_01972};
DE            EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE            Short=TO {ECO:0000255|HAMAP-Rule:MF_01972};
DE            Short=TRPO {ECO:0000255|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_01972};
GN   Name=kynA {ECO:0000255|HAMAP-Rule:MF_01972}; OrderedLocusNames=CC_2886;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC   -!- FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative
CC       cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-
CC       tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage
CC       of the indole moiety. {ECO:0000255|HAMAP-Rule:MF_01972}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tryptophan + O2 = N-formyl-L-kynurenine;
CC         Xref=Rhea:RHEA:24536, ChEBI:CHEBI:15379, ChEBI:CHEBI:57912,
CC         ChEBI:CHEBI:58629; EC=1.13.11.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01972};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01972};
CC       Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_01972};
CC   -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC       kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01972}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01972}.
CC   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01972}.
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DR   EMBL; AE005673; AAK24850.1; -; Genomic_DNA.
DR   PIR; F87606; F87606.
DR   RefSeq; NP_421682.1; NC_002696.2.
DR   RefSeq; WP_010920726.1; NC_002696.2.
DR   AlphaFoldDB; Q9A4E8; -.
DR   SMR; Q9A4E8; -.
DR   STRING; 190650.CC_2886; -.
DR   EnsemblBacteria; AAK24850; AAK24850; CC_2886.
DR   KEGG; ccr:CC_2886; -.
DR   PATRIC; fig|190650.5.peg.2890; -.
DR   eggNOG; COG3483; Bacteria.
DR   HOGENOM; CLU_063240_0_0_5; -.
DR   OMA; WRWRNDH; -.
DR   BioCyc; CAULO:CC2886-MON; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000001816; Chromosome.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; ISS:UniProtKB.
DR   HAMAP; MF_01972; T23O; 1.
DR   InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR   InterPro; IPR004981; Trp_2_3_dOase.
DR   PANTHER; PTHR10138; PTHR10138; 2.
DR   Pfam; PF03301; Trp_dioxygenase; 2.
DR   SUPFAM; SSF140959; SSF140959; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Tryptophan catabolism.
FT   CHAIN           1..263
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000360113"
FT   BINDING         32..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         221
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ   SEQUENCE   263 AA;  29919 MW;  17220BFF32FBA370 CRC64;
     MAQDMTYARY LALDELLSAQ KPLSDRHDEL LFIVIHQTKE LWLKEILHEV ALALKLIAGG
     DVEPAYKALA RVSRIQTVMT LSWDILATMT PADYLSFRDD LGTSSGFQSH QFRALEYLLG
     LKDQSFLKFH TERPEALAML KSALESPSLY DVAIAQLPRH GLTVPDAALH RDFSQTYVPS
     PEVEAAWLEV YRDPKRYWEL YQLAEKLVDL DDALVTWRHK HVLTVERIIG GRPGTGGTDG
     VGYLASTLRR RAFPELWSLR TKL
 
 
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