ID   HGD_PSE14               Reviewed;         435 AA.
AC   Q48GS7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   05-MAY-2009, entry version 24.
DE   RecName: Full=Homogentisate 1,2-dioxygenase;
DE            EC=1.13.11.5;
DE   AltName: Full=Homogentisicase;
DE   AltName: Full=Homogentisate oxygenase;
DE   AltName: Full=Homogentisic acid oxidase;
GN   Name=hmgA; OrderedLocusNames=PSPPH_3246;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
CC   -!- CATALYTIC ACTIVITY: Homogentisate + O(2) = 4-maleylacetoacetate.
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetic acid and fumarate from L-phenylalanine: step 4/6.
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
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DR   EMBL; CP000058; AAZ36498.1; -; Genomic_DNA.
DR   RefSeq; YP_275406.1; -.
DR   GeneID; 3559119; -.
DR   GenomeReviews; CP000058_GR; PSPPH_3246.
DR   KEGG; psp:PSPPH_3246; -.
DR   NMPDR; fig|264730.3.peg.3236; -.
DR   HOGENOM; Q48GS7; -.
DR   OMA; Q48GS7; HRNCMSE.
DR   GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:HAMAP.
DR   HAMAP; MF_00334; -; 1.
DR   InterPro; IPR005708; Homogentis_dOase.
DR   PANTHER; PTHR11056; Homogentis_dOase; 1.
DR   Pfam; PF04209; HgmA; 1.
DR   TIGRFAMs; TIGR01015; hmgA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Phenylalanine catabolism; Tyrosine catabolism.
FT   CHAIN         1    435       Homogentisate 1,2-dioxygenase.
FT                                /FTId=PRO_0000225793.
FT   METAL       332    332       Iron (By similarity).
FT   METAL       338    338       Iron (By similarity).
FT   METAL       368    368       Iron (By similarity).
SQ   SEQUENCE   435 AA;  48438 MW;  780C40AF83FC95C0 CRC64;
     MAIHSRSDAL AYQSGFGNQF SSEALPGALP IGQNSPQKHP LGLYAEQFSG TAFTVARSEA
     RRTWLYRIKP SAAHPRYQRM GRQIAGQEQG PINPNRLRWN AFDIPAEPVD FIDGLIPLAS
     TSAADQADGV SVYVYAANTS MQRAFFSADG EWLIVPQQGR LRIITELGLL DIEPLEIAVL
     PRGMKFRVQL LDSSARGYIC ENHGCALRLP ELGPIGSNGL ANPRDFLTPV AWFEDNQQPV
     ELVQKFLGEL WSTHLEHSPF DVVGWHGNNV AYKYDLRRFN TIGTVSYDHP DPSIFTVLTS
     PGAAHGQANI DFVIFPPRWM VAENTFRPPW FHRNLMNEFM GLIDGAYDAK AEGFMPGGAS
     LHNCMSAHGP DNVTAEKAIA AELKPHKIEN TMAFMFETGK VLRPSRHALG CPQLQADYDA
     CWNDMTRTFN KEPRR
//