3HAO_PSEFL
ID 3HAO_PSEFL Reviewed; 185 AA.
AC Q83V26;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_00825};
DE AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE Short=3-HAO {ECO:0000255|HAMAP-Rule:MF_00825};
DE AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE Short=HAD {ECO:0000255|HAMAP-Rule:MF_00825};
GN Name=nbaC {ECO:0000255|HAMAP-Rule:MF_00825};
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION,
RP COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP HIS-52 AND HIS-96.
RC STRAIN=KU-7;
RX PubMed=12620844; DOI=10.1128/aem.69.3.1564-1572.2003;
RA Muraki T., Taki M., Hasegawa Y., Iwaki H., Lau P.C.K.;
RT "Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-
RT dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in
RT the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain
RT KU-7.";
RL Appl. Environ. Microbiol. 69:1564-1572(2003).
CC -!- FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate
CC to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes
CC to quinolinate. {ECO:0000255|HAMAP-Rule:MF_00825,
CC ECO:0000269|PubMed:12620844}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate
CC 6-semialdehyde; Xref=Rhea:RHEA:17953, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:36559, ChEBI:CHEBI:77612; EC=1.13.11.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00825};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:12620844};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000305|PubMed:12620844};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+), Cu(2+) and Cd(2+).
CC {ECO:0000269|PubMed:12620844}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00825}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00825}.
CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC Rule:MF_00825}.
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DR EMBL; AB088043; BAC65311.1; -; Genomic_DNA.
DR AlphaFoldDB; Q83V26; -.
DR SMR; Q83V26; -.
DR BioCyc; MetaCyc:MON-13359; -.
DR BRENDA; 1.13.11.6; 5121.
DR UniPathway; UPA00253; UER00330.
DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd06123; cupin_HAO; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_00825; 3_HAO; 1.
DR InterPro; IPR010329; 3hydroanth_dOase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR15497; PTHR15497; 1.
DR Pfam; PF06052; 3-HAO; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW Oxidoreductase; Pyridine nucleotide biosynthesis.
FT CHAIN 1..185
FT /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT /id="PRO_0000245472"
FT BINDING 48
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT BINDING 52
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825"
FT MUTAGEN 52
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12620844"
FT MUTAGEN 96
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12620844"
SQ SEQUENCE 185 AA; 21245 MW; AC932875CC9D3D7D CRC64;
MMFTFGKPLN FQRWLDDHSD LLRPPVGNQQ VWQDSDFIVT VVGGPNFRTD FHDDPMEEFF
YQFKGNAYLN IMDRGQMDRV ELKEGDIFLL PPHLRHSPQR PEAGSRCLVI ERQRPKGMLD
GFEWYCLSCN GLVYRVDVQL NSIVTDLPPL FDIFYGNVGL RKCPQCGQVH PGKAAIEAVA
RGDQP
