ID   NICF_PSEPK              Reviewed;         213 AA.
AC   Q88FY5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Maleamate amidohydrolase;
DE            EC=3.5.1.107;
DE   AltName: Full=Nicotinate degradation protein F;
GN   Name=nicF; OrderedLocusNames=PP_3941;
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 BIOPHYSICOCHEMICAL PROPERTIES.
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: Maleamate amidase that transforms maleamate into maleate and
CC       ammonia in the aerobic nicotinate degradation pathway.
CC       {ECO:0000269|PubMed:18678916}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + maleamate = maleate + NH4(+); Xref=Rhea:RHEA:27385,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16146, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30780; EC=3.5.1.107;
CC         Evidence={ECO:0000269|PubMed:18678916};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=19.3 umol/min/mg enzyme {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   -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN69535.1; -; Genomic_DNA.
DR   RefSeq; NP_746071.1; NC_002947.4.
DR   RefSeq; WP_003251109.1; NC_002947.4.
DR   AlphaFoldDB; Q88FY5; -.
DR   SMR; Q88FY5; -.
DR   STRING; 160488.PP_3941; -.
DR   EnsemblBacteria; AAN69535; AAN69535; PP_3941.
DR   KEGG; ppu:PP_3941; -.
DR   PATRIC; fig|160488.4.peg.4196; -.
DR   eggNOG; COG1335; Bacteria.
DR   HOGENOM; CLU_068979_7_1_6; -.
DR   OMA; DVCNAYW; -.
DR   PhylomeDB; Q88FY5; -.
DR   BioCyc; MetaCyc:G1G01-4206-MON; -.
DR   BioCyc; PPUT160488:G1G01-4206-MON; -.
DR   SABIO-RK; Q88FY5; -.
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; 3.40.50.850; -; 1.
DR   InterPro; IPR000868; Isochorismatase-like.
DR   InterPro; IPR036380; Isochorismatase-like_sf.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   SUPFAM; SSF52499; SSF52499; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Hydrolase; Reference proteome.
FT   CHAIN           1..213
FT                   /note="Maleamate amidohydrolase"
FT                   /id="PRO_0000418470"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  22757 MW;  2D89BBAA6F65D717 CRC64;
     MSDAQSARDN YQGVWGQRIG FGRKPALLMI DFMQGYTTPG APLYAPGVVA AVEQAAGLLA
     LARDCGTLVV HTNIRYQPPH FADGGVWVRK APVMKDMVEG NPLAAFCEAV APQAGEVVLS
     KQYASAFFAT SLAPLLHAQG VDTVVLAGCS TSGCIRASAV DAMQHGFRTI VVRECVGDRH
     SDPHEANLFD IDSKYGDVVT RQDAMQQLRH LAG