NICX_PSEPK
ID NICX_PSEPK Reviewed; 350 AA.
AC Q88FY1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=2,5-dihydroxypyridine 5,6-dioxygenase;
DE Short=2,5-DHP dioxygenase;
DE EC=1.13.11.9;
DE AltName: Full=Nicotinate degradation protein X;
GN Name=nicX; OrderedLocusNames=PP_3945;
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 CATALYTIC ACTIVITY.
RX PubMed=5578917; DOI=10.1016/s0021-9258(18)62189-1;
RA Gauthier J.J., Rittenberg S.C.;
RT "The metabolism of nicotinic acid. I. Purification and properties of 2,5-
RT dihydroxypyridine oxygenase from Pseudomonas putida N-9.";
RL J. Biol. Chem. 246:3737-3742(1971).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=5578918; DOI=10.1016/s0021-9258(18)62190-8;
RA Gauthier J.J., Rittenberg S.C.;
RT "The metabolism of nicotinic acid. II. 2,5-dihydroxypyridine oxidation,
RT product formation, and oxygen 18 incorporation.";
RL J. Biol. Chem. 246:3743-3748(1971).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, 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).
CC -!- FUNCTION: Catalyzes the dioxygenolytic ring cleavage of 2,5-
CC dihydroxypyridine between carbons 5 and 6 generating N-formylmaleamate
CC in the aerobic nicotinate degradation pathway.
CC {ECO:0000269|PubMed:18678916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-dihydroxypyridine + O2 = H(+) + N-formylmaleamate;
CC Xref=Rhea:RHEA:27522, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16364, ChEBI:CHEBI:59911; EC=1.13.11.9;
CC Evidence={ECO:0000269|PubMed:18678916, ECO:0000269|PubMed:5578917,
CC ECO:0000269|PubMed:5578918};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:18678916};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for 2,5-dihydroxypyridine {ECO:0000269|PubMed:18678916};
CC Vmax=2.3 umol/min/mg enzyme {ECO:0000269|PubMed:18678916};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation.
CC {ECO:0000269|PubMed:18678916}.
CC -!- DISRUPTION PHENOTYPE: Cells lack 2,5-dihydroxypyridine 5,6-dioxygenase
CC activity. {ECO:0000269|PubMed:18678916}.
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DR EMBL; AE015451; AAN69539.1; -; Genomic_DNA.
DR RefSeq; NP_746075.1; NC_002947.4.
DR RefSeq; WP_004577272.1; NC_002947.4.
DR PDB; 7CN3; X-ray; 2.20 A; A/B/C/D/E/F=1-350.
DR PDB; 7CNT; X-ray; 2.28 A; A/B/C/D/E/F=1-350.
DR PDB; 7CUP; X-ray; 2.00 A; A/B/C/D/E/F=1-350.
DR PDBsum; 7CN3; -.
DR PDBsum; 7CNT; -.
DR PDBsum; 7CUP; -.
DR AlphaFoldDB; Q88FY1; -.
DR SMR; Q88FY1; -.
DR STRING; 160488.PP_3945; -.
DR EnsemblBacteria; AAN69539; AAN69539; PP_3945.
DR KEGG; ppu:PP_3945; -.
DR PATRIC; fig|160488.4.peg.4200; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_067564_0_0_6; -.
DR OMA; TCHIDIP; -.
DR PhylomeDB; Q88FY1; -.
DR BioCyc; MetaCyc:G1G01-4210-MON; -.
DR BioCyc; PPUT160488:G1G01-4210-MON; -.
DR SABIO-RK; Q88FY1; -.
DR UniPathway; UPA01010; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0047075; F:2,5-dihydroxypyridine 5,6-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..350
FT /note="2,5-dihydroxypyridine 5,6-dioxygenase"
FT /id="PRO_0000418469"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 318
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 320
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:7CUP"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:7CUP"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:7CNT"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:7CUP"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:7CUP"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:7CUP"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:7CUP"
SQ SEQUENCE 350 AA; 39017 MW; 0A0BCE5B1E54C3E6 CRC64;
MPVSNAQLTQ MFEHVLKLSR VDETQSVAVL KSHYSDPRTV NAAMEAAQRL KAKVYAVELP
AFNHPTAMGN DMTAYCGDTA LTGNLAAQRA LEAADLVVDT MMLLHSPEQE QILKTGTRIL
LAVEPPEVLA RMLPTEDDKR RVLAAETLLK QARSLHVRSK AGSDFHAPLG QYPAVTEYGY
ADEPGRWDHW PSGFLFTWPN EDSAEGTLVL DVGDIILPFK NYCRERITLE IEKGFITGIH
GGFEAEYLRD YMKYFNDPEV YGISHIGWGL QPRAQWTAMG LHDRNDGMCM DARAFYGNFL
FSTGPNTEVG GKRKTPCHLD IPLRNCDIYL DDKAVVLAGD VVAPEESRAR
