NICD_PSEPK
ID NICD_PSEPK Reviewed; 268 AA.
AC Q88FY3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=N-formylmaleamate deformylase;
DE EC=3.5.1.106;
DE AltName: Full=Nicotinate degradation protein D;
GN Name=nicD; OrderedLocusNames=PP_3943;
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 MUTAGENESIS OF SER-101; ASP-125;
RP GLU-221 AND HIS-245.
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).
CC -!- FUNCTION: Deformylase that catalyzes the conversion of N-formylmaleamic
CC acid to maleamate in the aerobic nicotinate degradation pathway.
CC {ECO:0000269|PubMed:18678916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-formylmaleamate = formate + H(+) + maleamate;
CC Xref=Rhea:RHEA:30843, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16146, ChEBI:CHEBI:59911;
CC EC=3.5.1.106; Evidence={ECO:0000269|PubMed:18678916};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation.
CC {ECO:0000269|PubMed:18678916}.
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 -!- DOMAIN: Shares some sequence similarities with the AB hydrolase
CC superfamily. {ECO:0000269|PubMed:18678916}.
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DR EMBL; AE015451; AAN69537.1; -; Genomic_DNA.
DR RefSeq; NP_746073.1; NC_002947.4.
DR RefSeq; WP_010954762.1; NC_002947.4.
DR AlphaFoldDB; Q88FY3; -.
DR SMR; Q88FY3; -.
DR STRING; 160488.PP_3943; -.
DR ESTHER; psepu-PP3943; NFM-deformylase.
DR EnsemblBacteria; AAN69537; AAN69537; PP_3943.
DR KEGG; ppu:PP_3943; -.
DR PATRIC; fig|160488.4.peg.4198; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_13_5_6; -.
DR OMA; ITWGFVA; -.
DR BioCyc; MetaCyc:G1G01-4208-MON; -.
DR BioCyc; PPUT160488:G1G01-4208-MON; -.
DR UniPathway; UPA01010; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Hydrolase; Reference proteome.
FT CHAIN 1..268
FT /note="N-formylmaleamate deformylase"
FT /id="PRO_0000418468"
FT DOMAIN 28..251
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 101
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT MUTAGEN 101
FT /note="S->A: Abolishes deformylase activity; when
FT associated with A-125 and A-245."
FT /evidence="ECO:0000269|PubMed:18678916"
FT MUTAGEN 125
FT /note="D->A: Abolishes deformylase activity; when
FT associated with A-101 and A-245."
FT /evidence="ECO:0000269|PubMed:18678916"
FT MUTAGEN 221
FT /note="E->A: Retains 70% of deformylase activity."
FT /evidence="ECO:0000269|PubMed:18678916"
FT MUTAGEN 245
FT /note="H->A: Abolishes deformylase activity; when
FT associated with A-101 and A-125."
FT /evidence="ECO:0000269|PubMed:18678916"
SQ SEQUENCE 268 AA; 29142 MW; 7D14BF0E5DAAF097 CRC64;
MSTFVAGGNV SANGIRQHYL RYGGKGHALI LVPGITSPAI TWGFVAERLG HYFDTYVLDV
RGRGLSSSGP DLDYGTDACA ADIPAFAAAL GLDSYHLLGH SMGARFAIRA AAQGAPGLQR
LVLVDPPVSG PGRRAYPSKL PWYVDSIRQA TVGMSGDDMR AFCATWSDEQ LALRAEWLHT
CYEPAIVRAF DDFHEVDIHQ YLPAVRQPAL LMVAGRGGVI EPRDIAEMRE LKPDIQVAYV
DNAGHMIPWD DLDGFFAAFG DFLDHPLV
