ID   Y1345_VIBCH             Reviewed;         378 AA.
AC   Q9KSB4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Putative dioxygenase VC_1345;
DE            EC=1.13.-.-;
GN   OrderedLocusNames=VC_1345;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE003852; AAF94503.1; -; Genomic_DNA.
DR   PIR; D82211; D82211.
DR   RefSeq; NP_230989.1; NC_002505.1.
DR   RefSeq; WP_000549756.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KSB4; -.
DR   SMR; Q9KSB4; -.
DR   STRING; 243277.VC_1345; -.
DR   DNASU; 2614799; -.
DR   EnsemblBacteria; AAF94503; AAF94503; VC_1345.
DR   GeneID; 57740007; -.
DR   KEGG; vch:VC_1345; -.
DR   PATRIC; fig|243277.26.peg.1282; -.
DR   eggNOG; COG3508; Bacteria.
DR   HOGENOM; CLU_053101_0_0_6; -.
DR   OMA; PYNHSNI; -.
DR   BioCyc; VCHO:VC1345-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR   GO; GO:0006570; P:tyrosine metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR005708; Homogentis_dOase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR11056; PTHR11056; 1.
DR   Pfam; PF04209; HgmA; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..378
FT                   /note="Putative dioxygenase VC_1345"
FT                   /id="PRO_0000220259"
FT   BINDING         288
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  43247 MW;  D0003F1F91D20707 CRC64;
     MHKWITFPHR EGTCSRQAHA DFPEQAIYER EAGRSGFFGP AAHFHHQHAP TGWSEWEGEL
     RPRAFNFNHV EGVNALSPWQ VPLLLHNHEV KVRVWKLEQA MPALARNADG DELLFIHQGK
     ADLYCDYGHM VVSEGDYALI PRSTNWRLEP IEPLFILMIE NTDAAYALPE KGLVGNHAVF
     DPAVLDVPSI NDQFRAQYSE QQTQVQVKRH GQLSTITFPF NPLDAVGWHG DLSVVRLNWR
     DIRPLMSHRY HLPPSAHTTF VGQGFVVCTF VPRPIESDPG ALKVPFYHNN DDYDEVLFYH
     AGDFFSRDNI EAGMVTFHPA GFTHGPHPKA FQAGLEYRKK FTDEVAVMID TRHALQFSDA
     AQQVENRQYV YSWQSKVE