3HAO_BOVIN
ID 3HAO_BOVIN Reviewed; 286 AA.
AC Q0VCA8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Name=HAAO {ECO:0000255|HAMAP-Rule:MF_03019};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 2-286, SUBUNIT, AND IRON-BINDING
RP SITES.
RX PubMed=19226621; DOI=10.1002/bip.21167;
RA Dilovic I., Gliubich F., Malpeli G., Zanotti G., Matkovic-Calogovic D.;
RT "Crystal structure of bovine 3-hydroxyanthranilate 3,4-dioxygenase.";
RL Biopolymers 91:1189-1195(2009).
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 -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_03019}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03019,
CC ECO:0000269|PubMed:19226621}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC Rule:MF_03019}.
CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC Rule:MF_03019}.
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DR EMBL; BC120265; AAI20266.1; -; mRNA.
DR RefSeq; NP_001068926.1; NM_001075458.2.
DR PDB; 3FE5; X-ray; 2.51 A; A=2-286.
DR PDBsum; 3FE5; -.
DR AlphaFoldDB; Q0VCA8; -.
DR SMR; Q0VCA8; -.
DR STRING; 9913.ENSBTAP00000006132; -.
DR PaxDb; Q0VCA8; -.
DR PeptideAtlas; Q0VCA8; -.
DR GeneID; 510602; -.
DR KEGG; bta:510602; -.
DR CTD; 23498; -.
DR eggNOG; KOG3995; Eukaryota.
DR HOGENOM; CLU_064845_1_0_1; -.
DR InParanoid; Q0VCA8; -.
DR OrthoDB; 1325876at2759; -.
DR TreeFam; TF300246; -.
DR BRENDA; 1.13.11.6; 908.
DR UniPathway; UPA00253; UER00330.
DR EvolutionaryTrace; Q0VCA8; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
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:0009435; P:NAD biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019805; P:quinolinate biosynthetic process; ISS:UniProtKB.
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; IPR016700; 3hydroanth_dOase_met.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR15497; PTHR15497; 1.
DR Pfam; PF06052; 3-HAO; 1.
DR PIRSF; PIRSF017681; 3hydroanth_dOase_animal; 1.
DR SUPFAM; SSF51182; SSF51182; 2.
DR TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..286
FT /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT /id="PRO_0000283033"
FT REGION 1..160
FT /note="Domain A (catalytic)"
FT REGION 161..177
FT /note="Linker"
FT REGION 178..286
FT /note="Domain B"
FT BINDING 43
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 47
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 53
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 91
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:3FE5"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:3FE5"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3FE5"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 24..41
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3FE5"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3FE5"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:3FE5"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:3FE5"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3FE5"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:3FE5"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:3FE5"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:3FE5"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3FE5"
SQ SEQUENCE 286 AA; 32493 MW; 6887DDB93B861F8E CRC64;
MERPVRVKAW VEENRGSFLP PVCNKLLHQK QLKIMFVGGP NTRKDYHIEE GEEVFYQLEG
DMLLRVLERG KHRDVVIRQG EIFLLPAGVP HSPQRFANTV GLVIERRRLK TELDGLRYYV
GDTTDVLFEK WFYCEDLGTQ LAPIIQEFFS SEQYRTGKPN PDQLLKEPPF PLSTRSVMEP
MCLEAWLDGH RKELQAGTPL SLFGDTYESQ VMVHGQGSSE GLRRDVDVWL WQLEGSSVVT
MEGQRLSLTL DDSLLVPAGT LYGWERGQGS VALSVTQDPA CKKSLG
