3HAO_NEMVE
ID 3HAO_NEMVE Reviewed; 272 AA.
AC A7RIT9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03019};
DE EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_03019};
DE AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000255|HAMAP-Rule:MF_03019};
DE Short=3-HAO {ECO:0000255|HAMAP-Rule:MF_03019};
DE AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000255|HAMAP-Rule:MF_03019};
DE Short=HAD {ECO:0000255|HAMAP-Rule:MF_03019};
GN ORFNames=v1g178517;
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6;
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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_03019}.
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_03019};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03019};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_03019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03019}.
CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC Rule:MF_03019}.
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DR EMBL; DS469513; EDO48567.1; -; Genomic_DNA.
DR RefSeq; XP_001640630.1; XM_001640580.1.
DR AlphaFoldDB; A7RIT9; -.
DR SMR; A7RIT9; -.
DR STRING; 45351.EDO48567; -.
DR EnsemblMetazoa; EDO48567; EDO48567; NEMVEDRAFT_v1g178517.
DR GeneID; 5520803; -.
DR KEGG; nve:5520803; -.
DR eggNOG; KOG3995; Eukaryota.
DR HOGENOM; CLU_064845_1_0_1; -.
DR InParanoid; A7RIT9; -.
DR OMA; WQMEGSS; -.
DR OrthoDB; 1325876at2759; -.
DR PhylomeDB; A7RIT9; -.
DR UniPathway; UPA00253; UER00330.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IBA:GO_Central.
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:0046874; P:quinolinate metabolic process; IBA:GO_Central.
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; 2.
DR TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..272
FT /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT /id="PRO_0000361973"
FT REGION 1..154
FT /note="Domain A (catalytic)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT REGION 155..169
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT REGION 170..272
FT /note="Domain B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 38
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 42
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 48
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
SQ SEQUENCE 272 AA; 31200 MW; EEE73F11A02CC7B1 CRC64;
MMEWIDENSS LFVPPVCNKL MYGEGQLKIM FVGGPNTRKD YHLEEGEELF FQVKGDMCLK
VLEKGKPKDI IIKEGEMFLL PSRFNHSPQR FENTVGLVIE RERLPEEIDG LRYFCEDGVT
VLWEKFFHCT DLTQIAPVIK EFFESEEHKT GKPSKESSCS INVDTETELM EPFPLKQWLK
DNKDSYRSGS MAIFEKGEFK VHAHGSGEQE GHSQGEMWFW QLEGKATVNV DEITRELNKN
DVLMITAGSD FRVKREEGSV GLSITVDSLA NK
