ID   MAIA_ALCFA              Reviewed;         253 AA.
AC   O24766;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 54.
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};
GN   Name=maiA {ECO:0000255|HAMAP-Rule:MF_00943};
OS   Alcaligenes faecalis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 8750 / DSM 30030 / CCUG 1814 / LMG 1229 / NBRC 13111 / NCIMB
RC   8156 / NCTC 11953 / Conn 16;
RX   PubMed=9345272; DOI=10.1006/bbrc.1997.7430;
RA   Hatakeyama K., Asai Y., Uchida Y., Kobayashi M., Terasawa M., Yukawa H.;
RT   "Gene cloning and characterization of maleate cis-trans isomerase from
RT   Alcaligenes faecalis.";
RL   Biochem. Biophys. Res. Commun. 239:74-79(1997).
RN   [2]
RP   MUTAGENESIS OF CYS-64; CYS-80 AND CYS-198.
RX   PubMed=10803955; DOI=10.1271/bbb.64.569;
RA   Hatakeyama K., Goto M., Uchida Y., Kobayashi M., Terasawa M., Yukawa H.;
RT   "Molecular analysis of maleate cis-trans isomerase from thermophilic
RT   bacteria.";
RL   Biosci. Biotechnol. Biochem. 64:569-576(2000).
CC   -!- FUNCTION: Catalyzes cis-trans isomerization of the C2-C3 double bond in
CC       maleate to yield fumarate. {ECO:0000255|HAMAP-Rule:MF_00943,
CC       ECO:0000269|PubMed:9345272}.
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, ECO:0000269|PubMed:9345272};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 uM for maleate {ECO:0000269|PubMed:9345272};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9345272}.
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; AB005051; BAA23002.1; -; Genomic_DNA.
DR   PIR; JC5709; JC5709.
DR   AlphaFoldDB; O24766; -.
DR   SMR; O24766; -.
DR   STRING; 511.JT27_07715; -.
DR   PRIDE; O24766; -.
DR   eggNOG; COG3473; Bacteria.
DR   BioCyc; MetaCyc:MON-20942; -.
DR   SABIO-RK; O24766; -.
DR   GO; GO:0050076; F:maleate isomerase activity; IDA:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA: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   1: Evidence at protein level;
KW   Isomerase.
FT   CHAIN           1..253
FT                   /note="Maleate isomerase"
FT                   /id="PRO_0000418471"
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         14
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"
FT   MUTAGEN         64
FT                   /note="C->S: Only slightly affects activity."
FT                   /evidence="ECO:0000269|PubMed:10803955"
FT   MUTAGEN         80
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10803955"
FT   MUTAGEN         198
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10803955"
SQ   SEQUENCE   253 AA;  27971 MW;  D0009123F7C00446 CRC64;
     MKTYRIGQIV PSSNTTMETE IPAMLQARYA EFPEERFTFH SSRMRMMHVN PEELKAMDIA
     SDRCAVELSD ARMSVMAYAC LVAIMAQGDG YHRVSQARLQ NTVKENGVEI PVLSSAGALV
     DTLKEFGYKK VSIITPYMKP LTKRVADYIE AEGIEVQDSI SLEVSDNLEV GLLNPENLLE
     HVKRLNHDGV DAVILSACVQ MPSLPAIQRA QDQIGKPVLS AAVWTVYQML KNLGLETRVP
     NAGHILSGVK PQA