MAIA_PSEPK
ID MAIA_PSEPK Reviewed; 250 AA.
AC Q88FY4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Maleate isomerase {ECO:0000255|HAMAP-Rule:MF_00943};
DE EC=5.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00943};
DE AltName: Full=Maleate cis-trans isomerase {ECO:0000255|HAMAP-Rule:MF_00943};
DE AltName: Full=Nicotinate degradation protein E;
GN Name=maiA {ECO:0000255|HAMAP-Rule:MF_00943}; Synonyms=nicE;
GN OrderedLocusNames=PP_3942;
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 PATHWAY, AND FUNCTION.
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: Catalyzes cis-trans isomerization of the C2-C3 double bond in
CC maleate to yield fumarate in the aerobic nicotinate degradation
CC pathway. {ECO:0000305|PubMed:18678916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=maleate = fumarate; Xref=Rhea:RHEA:13169, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30780; EC=5.2.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00943};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation.
CC {ECO:0000269|PubMed:18678916}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00943}.
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 -!- MISCELLANEOUS: Reaction is initiated by nucleophilic attack of cysteine
CC at the double bond, yielding a covalent succinylcysteine-like
CC intermediate. {ECO:0000255|HAMAP-Rule:MF_00943}.
CC -!- SIMILARITY: Belongs to the maleate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00943}.
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DR EMBL; AE015451; AAN69536.1; -; Genomic_DNA.
DR RefSeq; NP_746072.1; NC_002947.4.
DR RefSeq; WP_003251112.1; NC_002947.4.
DR AlphaFoldDB; Q88FY4; -.
DR SMR; Q88FY4; -.
DR STRING; 160488.PP_3942; -.
DR EnsemblBacteria; AAN69536; AAN69536; PP_3942.
DR KEGG; ppu:PP_3942; -.
DR PATRIC; fig|160488.4.peg.4197; -.
DR eggNOG; COG3473; Bacteria.
DR HOGENOM; CLU_068086_0_0_6; -.
DR OMA; NTTMEME; -.
DR PhylomeDB; Q88FY4; -.
DR BioCyc; MetaCyc:G1G01-4207-MON; -.
DR BioCyc; PPUT160488:G1G01-4207-MON; -.
DR UniPathway; UPA01010; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0050076; F:maleate isomerase activity; ISS:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR HAMAP; MF_00943; Maleate_isomerase; 1.
DR InterPro; IPR026286; MaiA/AMDase.
DR InterPro; IPR028615; Maleate_isomerase.
DR PANTHER; PTHR40267; PTHR40267; 1.
DR Pfam; PF17645; Amdase; 1.
DR PIRSF; PIRSF015736; MI; 1.
PE 2: Evidence at transcript level;
KW Aromatic hydrocarbons catabolism; Isomerase; Reference proteome.
FT CHAIN 1..250
FT /note="Maleate isomerase"
FT /id="PRO_0000418473"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT BINDING 80..82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT BINDING 199..200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT MOD_RES 80
FT /note="S-(2-succinyl)cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
SQ SEQUENCE 250 AA; 27003 MW; 87FA0727E05749E7 CRC64;
MTQLYRIGQI VPSSNTTMET EIPAMLNARQ AIRPERFTFH SSRMRMKQVK KEELAAMDAE
SDRCAVELSD AKVDVLGYAC LVAIMAMGLG YHRQSEKRLQ QATADNDALA PVITSAGALV
EALHVMKAKR IAIVAPYMKP LTELVVNYIR EEGFEVQDWR ALEIPDNLAV ARHDPANLPG
IVAGMDLEGV DVVVLSACVQ MQSLPAVAKV EAQTGKPVVT AAIATTYAML KALDLEPIVP
GAGALLSGAY
