(data stored in SCRATCH zone)

SWISSPROT: C6WFA3_ACTMD

ID   C6WFA3_ACTMD            Unreviewed;       273 AA.
AC   C6WFA3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01972};
DE            Short=TDO {ECO:0000256|HAMAP-Rule:MF_01972};
DE            EC=1.13.11.11 {ECO:0000256|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophan oxygenase {ECO:0000256|HAMAP-Rule:MF_01972};
DE            Short=TO {ECO:0000256|HAMAP-Rule:MF_01972};
DE            Short=TRPO {ECO:0000256|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophan pyrrolase {ECO:0000256|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophanase {ECO:0000256|HAMAP-Rule:MF_01972};
GN   Name=kynA {ECO:0000256|HAMAP-Rule:MF_01972};
GN   OrderedLocusNames=Amir_0266 {ECO:0000313|EMBL:ACU34235.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34235.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34235.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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
CC       cleavage of the indole moiety. {ECO:0000256|HAMAP-Rule:MF_01972}.
CC   -!- CATALYTIC ACTIVITY: L-tryptophan + O(2) = N-formyl-L-kynurenine.
CC       {ECO:0000256|HAMAP-Rule:MF_01972}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01972};
CC       Note=Binds 1 heme group per subunit. {ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-Rule:MF_01972}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01972}.
CC   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01972}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01972}.
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DR   EMBL; CP001630; ACU34235.1; -; Genomic_DNA.
DR   RefSeq; WP_012782898.1; NC_013093.1.
DR   ProteinModelPortal; C6WFA3; -.
DR   STRING; 446462.Amir_0266; -.
DR   EnsemblBacteria; ACU34235; ACU34235; Amir_0266.
DR   KEGG; ami:Amir_0266; -.
DR   eggNOG; ENOG4105HJ8; Bacteria.
DR   eggNOG; COG3483; LUCA.
DR   HOGENOM; HOG000221583; -.
DR   KO; K00453; -.
DR   OMA; YWDLYQL; -.
DR   OrthoDB; POG091H0DJ4; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01972; T23O; 1.
DR   InterPro; IPR004981; Trp_2_3_dOase.
DR   PANTHER; PTHR10138; PTHR10138; 1.
DR   Pfam; PF03301; Trp_dioxygenase; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WFA3.
DR   SWISS-2DPAGE; C6WFA3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Dioxygenase {ECO:0000256|HAMAP-Rule:MF_01972,
KW   ECO:0000313|EMBL:ACU34235.1}; Heme {ECO:0000256|HAMAP-Rule:MF_01972};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01972};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01972};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01972};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Tryptophan catabolism {ECO:0000256|HAMAP-Rule:MF_01972}.
FT   METAL       231    231       Iron (heme axial ligand).
FT                                {ECO:0000256|HAMAP-Rule:MF_01972}.
FT   BINDING     110    110       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01972}.
FT   BINDING     245    245       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01972}.
SQ   SEQUENCE   273 AA;  31020 MW;  F340CCB5C87153B4 CRC64;
     MEQVCPVAPK LDFGGTTPYE DYVRASVLHT LQRQASDDPR EMSFLVTTQV MELYFGLLCF
     EWRQAQKELR ADDVTAAVRT LRRSELHMQA LNAAWRPIAR MTPGEFNSFR DALGEGSGFQ
     SGRYREVEFL LGEKSRSMLV PHRSAPAQHD ALEALLSEPS LYDDVLAALH RRGLDVPDEL
     LKRDFAEAYA PDERVEAVWA HVYREGPRDL LELGEALTDV AEEFSRWRHD HLLATRRSMG
     SKVGTGGSAG VAWLEKRVRR AVFPELWTAR SYV
//

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