HGD_PONAB
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 03-AUG-2022, entry version 78.
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; 795654at2759; -.
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 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.
DR TIGRFAMs; TIGR01015; hmgA; 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