HGD_NITHX
ID HGD_NITHX Reviewed; 448 AA.
AC Q1QPR8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Homogentisate 1,2-dioxygenase {ECO:0000255|HAMAP-Rule:MF_00334};
DE Short=HGDO {ECO:0000255|HAMAP-Rule:MF_00334};
DE EC=1.13.11.5 {ECO:0000255|HAMAP-Rule:MF_00334};
DE AltName: Full=Homogentisate oxygenase {ECO:0000255|HAMAP-Rule:MF_00334};
DE AltName: Full=Homogentisic acid oxidase {ECO:0000255|HAMAP-Rule:MF_00334};
DE AltName: Full=Homogentisicase {ECO:0000255|HAMAP-Rule:MF_00334};
GN Name=hmgA {ECO:0000255|HAMAP-Rule:MF_00334}; OrderedLocusNames=Nham_0921;
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the catabolism of homogentisate (2,5-
CC dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the
CC degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring
CC cleavage of the aromatic ring of homogentisate to yield
CC maleylacetoacetate. {ECO:0000255|HAMAP-Rule:MF_00334}.
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:0000255|HAMAP-Rule:MF_00334};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00334};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 4/6.
CC {ECO:0000255|HAMAP-Rule:MF_00334}.
CC -!- SUBUNIT: Hexamer; dimer of trimers. {ECO:0000255|HAMAP-Rule:MF_00334}.
CC -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00334}.
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DR EMBL; CP000319; ABE61779.1; -; Genomic_DNA.
DR RefSeq; WP_011509475.1; NC_007964.1.
DR AlphaFoldDB; Q1QPR8; -.
DR SMR; Q1QPR8; -.
DR STRING; 323097.Nham_0921; -.
DR EnsemblBacteria; ABE61779; ABE61779; Nham_0921.
DR KEGG; nha:Nham_0921; -.
DR eggNOG; COG3508; Bacteria.
DR HOGENOM; CLU_027174_0_0_5; -.
DR OMA; FMFETRW; -.
DR OrthoDB; 193687at2; -.
DR UniPathway; UPA00139; UER00339.
DR Proteomes; UP000001953; Chromosome.
DR GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_00334; Homogentis_dioxygen; 1.
DR InterPro; IPR005708; Homogentis_dOase.
DR InterPro; IPR022950; Homogentis_dOase_bac.
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 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Reference proteome; Tyrosine catabolism.
FT CHAIN 1..448
FT /note="Homogentisate 1,2-dioxygenase"
FT /id="PRO_1000019531"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 346
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 352
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 361
FT /ligand="homogentisate"
FT /ligand_id="ChEBI:CHEBI:16169"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 382
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 382
FT /ligand="homogentisate"
FT /ligand_id="ChEBI:CHEBI:16169"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
SQ SEQUENCE 448 AA; 49674 MW; 1E4007C93C156DCA CRC64;
MNTSFDPVAA NSNSANVTPG YMSGFGNSFE TEALPGALPI GRNSPQRCAY GLYAEQLSGS
PFTAPRGANE RSWLYRIRPS VRHSGHFVKI DAKLWRTAPC LEHDMPLAQL RWDPTPIPED
ELTFVQSVRT MTTAGDAHTQ TGMAAHIYLI TRSMVDQHFY NADGEMLFVP QGGSLRFVTE
FGVIDTEPGE IAVIPRGVKF RVEIPSGPAR GYLCENYGGA FTLPERGPIG ANCLANSRDF
LTPVAAYEDD DKPTELFVKW GGALWSTALP HSPIDVVAWH GNYAPYKYDL RTFSPIGAIG
FDHPDPSIFT VLTSPSEIAG TANIDFVIFP ERWVVAENTF RPPWYHMNVM SEFMGLIYGV
YDAKPQGFVP GGISLHNCML PHGPDREAFD HASNTELKPV KLTGTLAFMF ETRFPQRVTE
YAATSDALQD DYADCWQGLE RRFDPTRP
