DHPH_PAENI
ID DHPH_PAENI Reviewed; 397 AA.
AC Q93NG3;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=2,6-dihydroxypyridine 3-monooxygenase;
DE Short=2,6-DHPH;
DE EC=1.14.13.10;
GN Name=dhpH;
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=11514508; DOI=10.1128/jb.183.18.5262-5267.2001;
RA Baitsch D., Sandu C., Brandsch R., Igloi G.L.;
RT "Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in
RT degradation of the plant alkaloid nicotine: cloning, purification, and
RT characterization of 2,6-dihydroxypyridine 3-hydroxylase.";
RL J. Bacteriol. 183:5262-5267(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=12618462; DOI=10.1128/jb.185.6.1976-1986.2003;
RA Igloi G.L., Brandsch R.;
RT "Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter
RT nicotinovorans and identification of a pAO1-dependent nicotine uptake
RT system.";
RL J. Bacteriol. 185:1976-1986(2003).
RN [3]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FAD, AND MUTAGENESIS
RP OF CYS-323.
RX PubMed=18440023; DOI=10.1016/j.jmb.2008.03.032;
RA Treiber N., Schulz G.E.;
RT "Structure of 2,6-dihydroxypyridine 3-hydroxylase from a nicotine-degrading
RT pathway.";
RL J. Mol. Biol. 379:94-104(2008).
CC -!- FUNCTION: Catalyzes the conversion of 2,6-dihydroxypyridine into 2,3,6-
CC trihydroxypyridine in the nicotine degradation pathway.
CC {ECO:0000269|PubMed:11514508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6-dihydroxypyridine + H(+) + NADH + O2 = 2,3,6-
CC trihydroxypyridine + H2O + NAD(+); Xref=Rhea:RHEA:16917,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16683, ChEBI:CHEBI:17681, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.13.10;
CC Evidence={ECO:0000269|PubMed:11514508};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11514508};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0000083 M for 2,6-dihydroxypyridine
CC {ECO:0000269|PubMed:11514508};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:11514508};
CC Temperature dependence:
CC Optimum temperature is 20 degrees Celsius.
CC {ECO:0000269|PubMed:11514508};
CC -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC {ECO:0000269|PubMed:11514508}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11514508,
CC ECO:0000269|PubMed:18440023}.
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DR EMBL; AF373840; AAK64255.1; -; Genomic_DNA.
DR EMBL; AJ507836; CAD47937.1; -; Genomic_DNA.
DR RefSeq; WP_016359448.1; NC_021229.1.
DR RefSeq; YP_007988763.1; NC_021229.1.
DR PDB; 2VOU; X-ray; 2.60 A; A/B/C=1-397.
DR PDBsum; 2VOU; -.
DR AlphaFoldDB; Q93NG3; -.
DR SMR; Q93NG3; -.
DR KEGG; ag:AAK64255; -.
DR BioCyc; MetaCyc:MON-1001; -.
DR BRENDA; 1.14.13.10; 449.
DR SABIO-RK; Q93NG3; -.
DR UniPathway; UPA00106; -.
DR EvolutionaryTrace; Q93NG3; -.
DR GO; GO:0018663; F:2,6-dihydroxypyridine 3-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019608; P:nicotine catabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; NAD; Nucleotide-binding; Oxidoreductase;
KW Plasmid.
FT CHAIN 1..397
FT /note="2,6-dihydroxypyridine 3-monooxygenase"
FT /id="PRO_0000430255"
FT BINDING 14..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18440023"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18440023"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18440023"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18440023"
FT BINDING 306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18440023"
FT BINDING 316..320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18440023"
FT MUTAGEN 323
FT /note="C->S: Does not cause structural disturbance."
FT /evidence="ECO:0000269|PubMed:18440023"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2VOU"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 318..335
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 339..368
FT /evidence="ECO:0007829|PDB:2VOU"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:2VOU"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2VOU"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:2VOU"
SQ SEQUENCE 397 AA; 43400 MW; D257CDC11D516CBE CRC64;
MSPTTDRIAV VGGSISGLTA ALMLRDAGVD VDVYERSPQP LSGFGTGIVV QPELVHYLLE
QGVELDSISV PSSSMEYVDA LTGERVGSVP ADWRFTSYDS IYGGLYELFG PERYHTSKCL
VGLSQDSETV QMRFSDGTKA EANWVIGADG GASVVRKRLL GIEPTYAGYV TWRGVLQPGE
VADDVWNYFN DKFTYGLLDD GHLIAYPIPG RENAESPRLN FQWYWNVAEG PDLDELMTDV
RGIRLPTSVH NNSLNPHNLR QFHSKGESLF KPFRDLVLNA SSPFVTVVAD ATVDRMVHGR
VLLIGDAAVT PRPHAAAGGA KACDDARTLA EVFTKNHDLR GSLQSWETRQ LQQGHAYLNK
VKKMASRLQH GGSFEPGNPA FAFGLPKVDE PSVVTNS
