3HAO_CUPMC
ID 3HAO_CUPMC Reviewed; 174 AA.
AC Q1LCS4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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}; OrderedLocusNames=Rmet_5193;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15909977; DOI=10.1021/bi0473455;
RA Colabroy K.L., Zhai H., Li T., Ge Y., Zhang Y., Liu A., Ealick S.E.,
RA McLafferty F.W., Begley T.P.;
RT "The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by
RT 4-chloro-3-hydroxyanthranilate.";
RL Biochemistry 44:7623-7631(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH
RP SUBSTRATES OR INHIBITOR AND IRON, COFACTOR, KINETIC PARAMETERS, MUTAGENESIS
RP OF ARG-47; ARG-99 AND GLU-110, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=15909978; DOI=10.1021/bi047353l;
RA Zhang Y., Colabroy K.L., Begley T.P., Ealick S.E.;
RT "Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic
RT mechanism of a complex oxidation involved in NAD biosynthesis.";
RL Biochemistry 44:7632-7643(2005).
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:15909977}.
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:0000255|HAMAP-Rule:MF_00825,
CC ECO:0000269|PubMed:15909978};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00825,
CC ECO:0000269|PubMed:15909978};
CC -!- ACTIVITY REGULATION: Inhibited by 4-chloro-3-hydroxyanthranilate.
CC Mechanism of inactivation involves the oxidation of the catalytic
CC active site Fe(2+) to the catalytically inactive Fe(3+) oxidation
CC state, superoxide production, and formation of two disulfide bonds
CC between Cys-125 and Cys-128, and Cys-162 and Cys-165. Enzyme can be
CC reactivated under reducing conditions. {ECO:0000269|PubMed:15909977}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.4 uM for 3-hydroxyanthranilate {ECO:0000269|PubMed:15909978};
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 ECO:0000269|PubMed:15909978}.
CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC Rule:MF_00825}.
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DR EMBL; CP000353; ABF12052.1; -; Genomic_DNA.
DR RefSeq; WP_011519599.1; NC_007974.2.
DR PDB; 1YFU; X-ray; 1.90 A; A=1-174.
DR PDB; 1YFW; X-ray; 2.00 A; A=1-174.
DR PDB; 1YFX; X-ray; 2.00 A; A=1-174.
DR PDB; 1YFY; X-ray; 3.20 A; A=1-174.
DR PDB; 4HSJ; X-ray; 1.88 A; A=1-174.
DR PDB; 4HSL; X-ray; 2.00 A; A=1-174.
DR PDB; 4HVO; X-ray; 1.75 A; A=1-174.
DR PDB; 4HVQ; X-ray; 2.81 A; A=1-154.
DR PDB; 4HVR; X-ray; 2.70 A; A=1-174.
DR PDB; 4I3P; X-ray; 1.96 A; A=1-174.
DR PDB; 4L2N; X-ray; 1.74 A; A=1-174.
DR PDB; 4R52; X-ray; 1.53 A; A=1-174.
DR PDB; 4WZC; X-ray; 1.84 A; A=1-174.
DR PDB; 5V26; X-ray; 1.79 A; A/B=1-174.
DR PDB; 5V27; X-ray; 2.35 A; A=1-174.
DR PDB; 5V28; X-ray; 2.72 A; A=1-174.
DR PDB; 6BVP; X-ray; 1.90 A; A=1-174.
DR PDB; 6BVQ; X-ray; 2.08 A; A=1-174.
DR PDB; 6BVR; X-ray; 1.90 A; A=1-174.
DR PDB; 6BVS; X-ray; 2.32 A; A=1-174.
DR PDB; 6CD3; X-ray; 2.61 A; A=1-174.
DR PDB; 6D60; X-ray; 2.22 A; A=1-174.
DR PDB; 6D61; X-ray; 1.74 A; A=1-174.
DR PDB; 6D62; X-ray; 1.77 A; A=1-174.
DR PDB; 6VI5; X-ray; 1.60 A; A=1-174.
DR PDB; 6VI6; X-ray; 1.90 A; A=1-174.
DR PDB; 6VI7; X-ray; 2.62 A; A=1-174.
DR PDB; 6VI8; X-ray; 1.95 A; A=1-174.
DR PDB; 6VI9; X-ray; 2.31 A; A=1-174.
DR PDB; 6VIA; X-ray; 1.59 A; A=1-174.
DR PDB; 6VIB; X-ray; 1.84 A; A=1-174.
DR PDB; 6X11; X-ray; 2.10 A; A=1-174.
DR PDBsum; 1YFU; -.
DR PDBsum; 1YFW; -.
DR PDBsum; 1YFX; -.
DR PDBsum; 1YFY; -.
DR PDBsum; 4HSJ; -.
DR PDBsum; 4HSL; -.
DR PDBsum; 4HVO; -.
DR PDBsum; 4HVQ; -.
DR PDBsum; 4HVR; -.
DR PDBsum; 4I3P; -.
DR PDBsum; 4L2N; -.
DR PDBsum; 4R52; -.
DR PDBsum; 4WZC; -.
DR PDBsum; 5V26; -.
DR PDBsum; 5V27; -.
DR PDBsum; 5V28; -.
DR PDBsum; 6BVP; -.
DR PDBsum; 6BVQ; -.
DR PDBsum; 6BVR; -.
DR PDBsum; 6BVS; -.
DR PDBsum; 6CD3; -.
DR PDBsum; 6D60; -.
DR PDBsum; 6D61; -.
DR PDBsum; 6D62; -.
DR PDBsum; 6VI5; -.
DR PDBsum; 6VI6; -.
DR PDBsum; 6VI7; -.
DR PDBsum; 6VI8; -.
DR PDBsum; 6VI9; -.
DR PDBsum; 6VIA; -.
DR PDBsum; 6VIB; -.
DR PDBsum; 6X11; -.
DR AlphaFoldDB; Q1LCS4; -.
DR SMR; Q1LCS4; -.
DR STRING; 266264.Rmet_5193; -.
DR DrugBank; DB04598; 2-AMINO-4-CHLORO-3-HYDROXYBENZOIC ACID.
DR EnsemblBacteria; ABF12052; ABF12052; Rmet_5193.
DR KEGG; rme:Rmet_5193; -.
DR eggNOG; COG1917; Bacteria.
DR HOGENOM; CLU_095765_0_0_4; -.
DR OMA; NARKDYH; -.
DR OrthoDB; 1591291at2; -.
DR SABIO-RK; Q1LCS4; -.
DR UniPathway; UPA00253; UER00330.
DR EvolutionaryTrace; Q1LCS4; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
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 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Plasmid;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..174
FT /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT /id="PRO_0000245477"
FT BINDING 47
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 57
FT /ligand="substrate"
FT BINDING 95
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 99
FT /ligand="substrate"
FT BINDING 110
FT /ligand="substrate"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT MUTAGEN 47
FT /note="R->A: Increases KM for 3-hydroxyanthranilate 7-fold.
FT Decreases activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:15909978"
FT MUTAGEN 99
FT /note="R->A: Increases KM for 3-hydroxyanthranilate 40-
FT fold. Decreases activity 5000-fold."
FT /evidence="ECO:0000269|PubMed:15909978"
FT MUTAGEN 110
FT /note="E->A: Decreases KM for 3-hydroxyanthranilate 2-fold.
FT Decreases activity 2000-fold."
FT /evidence="ECO:0000269|PubMed:15909978"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:4R52"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4R52"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6VIA"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:4R52"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:4R52"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4R52"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:4R52"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:4R52"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:4R52"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4R52"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1YFW"
SQ SEQUENCE 174 AA; 20028 MW; 385F2E3DEB3947B8 CRC64;
MLTYGAPFNF PRWIDEHAHL LKPPVGNRQV WQDSDFIVTV VGGPNHRTDY HDDPLEEFFY
QLRGNAYLNL WVDGRRERAD LKEGDIFLLP PHVRHSPQRP EAGSACLVIE RQRPAGMLDG
FEWYCDACGH LVHRVEVQLK SIVTDLPPLF ESFYASEDKR RCPHCGQVHP GRAA
