ID   HGD_PONAB               Reviewed;         445 AA.
AC   Q5RF05;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   13-SEP-2023, entry version 81.
DE   RecName: Full=Homogentisate 1,2-dioxygenase;
DE            EC=1.13.11.5 {ECO:0000250|UniProtKB:Q93099};
DE   AltName: Full=Homogentisate oxygenase;
DE   AltName: Full=Homogentisic acid oxidase;
DE   AltName: Full=Homogentisicase;
GN   Name=HGD;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of homogentisate to
CC       maleylacetoacetate. {ECO:0000250|UniProtKB:Q93099}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=homogentisate + O2 = 4-maleylacetoacetate + H(+);
CC         Xref=Rhea:RHEA:15449, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16169, ChEBI:CHEBI:17105; EC=1.13.11.5;
CC         Evidence={ECO:0000250|UniProtKB:Q93099};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15450;
CC         Evidence={ECO:0000250|UniProtKB:Q93099};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q93099};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 4/6.
CC   -!- SUBUNIT: Homohexamer arranged as a dimer of trimers.
CC       {ECO:0000250|UniProtKB:Q93099}.
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; CR857357; CAH89652.1; -; mRNA.
DR   RefSeq; NP_001124743.1; NM_001131271.2.
DR   AlphaFoldDB; Q5RF05; -.
DR   SMR; Q5RF05; -.
DR   STRING; 9601.ENSPPYP00000015100; -.
DR   GeneID; 100171592; -.
DR   KEGG; pon:100171592; -.
DR   CTD; 3081; -.
DR   eggNOG; KOG1417; Eukaryota.
DR   InParanoid; Q5RF05; -.
DR   OrthoDB; 525at2759; -.
DR   UniPathway; UPA00139; UER00339.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07000; cupin_HGO_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR046451; HgmA_C.
DR   InterPro; IPR046452; HgmA_N.
DR   InterPro; IPR005708; Homogentis_dOase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   NCBIfam; TIGR01015; hmgA; 1.
DR   PANTHER; PTHR11056; HOMOGENTISATE 1,2-DIOXYGENASE; 1.
DR   PANTHER; PTHR11056:SF0; HOMOGENTISATE 1,2-DIOXYGENASE; 1.
DR   Pfam; PF04209; HgmA_C; 1.
DR   Pfam; PF20510; HgmA_N; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Phenylalanine catabolism; Reference proteome; Tyrosine catabolism.
FT   CHAIN           1..445
FT                   /note="Homogentisate 1,2-dioxygenase"
FT                   /id="PRO_0000314969"
FT   BINDING         335
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q93099"
FT   BINDING         341
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q93099"
FT   BINDING         371
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q93099"
FT   MOD_RES         98
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93099"
FT   MOD_RES         414
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O09173"
SQ   SEQUENCE   445 AA;  49911 MW;  2A7475FF04FC3A43 CRC64;
     MAQLKYISGF GNECSSEDPR CPGSLPEGQN NPQVCPYNLY AEQLSGSAFT CPRSTNKRSW
     LYRIPPSVSH KPFESIDEGH VTHNWDEVDP DPNQLRWKPF EIPKVSQKKV DLVSGLHTLC
     GAGDIKSNNG LAIHIFLCNT SMENRCFYNS DGDFLIVPQK GNLLIYTEFG KMLVQPNEIC
     VIQRGMRFSI DVFEETRGYI LEVYGVHFEL PDLGPIGANG LANPRDFLIP VAWYEDRQVP
     GGYTVIDKYQ GKLFAAKQGV SPFNVVAWHG NYTPYKYNLK NFMVINSVAF DHADPSIFTV
     LTAKSVRPGV AIADFVIFPP RWGVADKTFR PPYYHRNCMS EFMGLIRGHY EAKQGGFLPG
     GGSLHSTMTP HGPDADCFEK ASKAKLAPER IADGTMAFMF ESSLSLAVTK WGLKASRCLD
     ENYHKCWEPL KSHFTPNFRN PAEPN
//