6HN3M_PSEPK
ID 6HN3M_PSEPK Reviewed; 382 AA.
AC Q88FY2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=6-hydroxynicotinate 3-monooxygenase {ECO:0000303|PubMed:27218267};
DE Short=6-HNA monooxygenase {ECO:0000303|PubMed:27218267};
DE EC=1.14.13.114 {ECO:0000269|PubMed:18678916, ECO:0000269|PubMed:27218267};
DE AltName: Full=Nicotinate degradation protein C;
DE Flags: Precursor;
GN Name=nicC {ECO:0000303|PubMed:27218267}; OrderedLocusNames=PP_3944;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=18678916; DOI=10.1073/pnas.0802273105;
RA Jimenez J.I., Canales A., Jimenez-Barbero J., Ginalski K., Rychlewski L.,
RA Garcia J.L., Diaz E.;
RT "Deciphering the genetic determinants for aerobic nicotinic acid
RT degradation: the nic cluster from Pseudomonas putida KT2440.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11329-11334(2008).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=21450002; DOI=10.1111/j.1462-2920.2011.02471.x;
RA Jimenez J.I., Juarez J.F., Garcia J.L., Diaz E.;
RT "A finely tuned regulatory circuit of the nicotinic acid degradation
RT pathway in Pseudomonas putida.";
RL Environ. Microbiol. 13:1718-1732(2011).
RN [4] {ECO:0007744|PDB:5EOW}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FAD, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND
RP PATHWAY.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=27218267; DOI=10.1021/acs.biochem.6b00105;
RA Hicks K.A., Yuen M.E., Zhen W.F., Gerwig T.J., Story R.W., Kopp M.C.,
RA Snider M.J.;
RT "Structural and Biochemical Characterization of 6-Hydroxynicotinic Acid 3-
RT Monooxygenase, A Novel Decarboxylative Hydroxylase Involved in Aerobic
RT Nicotinate Degradation.";
RL Biochemistry 55:3432-3446(2016).
CC -!- FUNCTION: Flavin-dependent monooxygenase (FMO) that catalyzes the
CC decarboxylative hydroxylation of 6-hydroxynicotinic acid (6-HNA) to
CC 2,5-dihydroxypyridine (2,5-DHP) with concomitant oxidation of NADH, a
CC step in the aerobic nicotinate degradation pathway.
CC {ECO:0000269|PubMed:18678916, ECO:0000269|PubMed:27218267}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxynicotinate + 2 H(+) + NADH + O2 = 2,5-
CC dihydroxypyridine + CO2 + H2O + NAD(+); Xref=Rhea:RHEA:27333,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16364, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57664, ChEBI:CHEBI:57945; EC=1.14.13.114;
CC Evidence={ECO:0000269|PubMed:18678916, ECO:0000269|PubMed:27218267};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:27218267};
CC Note=Binds 1 FAD molecule per subunit. {ECO:0000269|PubMed:27218267};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=97 uM for 6-hydroxynicotinate (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:27218267};
CC KM=3 uM for NADH (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:27218267};
CC Note=kcat is 2.2 sec(-1) with 6-hydroxynicotinate as substrate (at pH
CC 7.5 and 25 degrees Celsius). {ECO:0000269|PubMed:27218267};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation.
CC {ECO:0000269|PubMed:18678916, ECO:0000305|PubMed:27218267}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27218267}.
CC -!- INDUCTION: Repressed by NicR in the absence of 6-hydroxynicotinate
CC (6HNA) inducer. In presence of 6HNA, repression is alleviated.
CC {ECO:0000269|PubMed:21450002}.
CC -!- DISRUPTION PHENOTYPE: Cells show a complete conversion of nicotinate to
CC 6-hydroxynicotinate. {ECO:0000269|PubMed:18678916}.
CC -!- SIMILARITY: Belongs to the 6-hydroxynicotinate 3-monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AE015451; AAN69538.1; -; Genomic_DNA.
DR RefSeq; NP_746074.1; NC_002947.4.
DR RefSeq; WP_010954763.1; NC_002947.4.
DR PDB; 5EOW; X-ray; 2.10 A; A=1-382.
DR PDBsum; 5EOW; -.
DR AlphaFoldDB; Q88FY2; -.
DR SMR; Q88FY2; -.
DR STRING; 160488.PP_3944; -.
DR EnsemblBacteria; AAN69538; AAN69538; PP_3944.
DR KEGG; ppu:PP_3944; -.
DR PATRIC; fig|160488.4.peg.4199; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_19_5_6; -.
DR OMA; SVWAIFD; -.
DR PhylomeDB; Q88FY2; -.
DR BioCyc; MetaCyc:G1G01-4209-MON; -.
DR BioCyc; PPUT160488:G1G01-4209-MON; -.
DR BRENDA; 1.14.13.114; 5092.
DR UniPathway; UPA01010; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0043731; F:6-hydroxynicotinate 3-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
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; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
KW Monooxygenase; NAD; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..382
FT /note="6-hydroxynicotinate 3-monooxygenase"
FT /id="PRO_0000418466"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3LKL4"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3LKL4"
FT BINDING 15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27218267,
FT ECO:0007744|PDB:5EOW"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27218267,
FT ECO:0007744|PDB:5EOW"
FT BINDING 47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27218267,
FT ECO:0007744|PDB:5EOW"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27218267,
FT ECO:0007744|PDB:5EOW"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27218267,
FT ECO:0007744|PDB:5EOW"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27218267,
FT ECO:0007744|PDB:5EOW"
FT BINDING 307..308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27218267,
FT ECO:0007744|PDB:5EOW"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:5EOW"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:5EOW"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:5EOW"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 306..324
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 329..353
FT /evidence="ECO:0007829|PDB:5EOW"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:5EOW"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:5EOW"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:5EOW"
SQ SEQUENCE 382 AA; 42694 MW; 0EB72444137FED72 CRC64;
MRGRQKIAIV GAGLGGAAAA TLLQQAGFDV EVFEQAPAFT RLGAGIHIGP NVMKIFRRMG
LEQKLELMGS HPDFWFSRDG NTGDYLSRIP LGEFARREYG AAYITIHRGD LHALQIEAIQ
PGTVHFGKRL EKIVDEGDQV RLDFADGTHT VADIVIGADG IHSKIREELL GAEAPIYSGW
VAHRALIRGV NLAQHADVFE PCVKWWSEDR HMMVYYTTGK RDEYYFVTGV PHEAWDFQGA
FVDSSQEEMR AAFEGYHPTV QKLIDATESI TKWPLRNRNP LPLWSRGRLV LLGDACHPMK
PHMAQGACMA IEDAAMLTRC LQETGLSDHR TAFALYEANR KERASQVQSV SNANTWLYSQ
EDPAWVYGYD LYGQQLESGE AA
