ID   MAIA_GEOSE              Reviewed;         251 AA.
AC   Q9WX57;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 53.
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   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=MI-102;
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:10803955}.
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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00943}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB015134; BAA77296.1; -; Genomic_DNA.
DR   PIR; JC7225; JC7225.
DR   AlphaFoldDB; Q9WX57; -.
DR   SMR; Q9WX57; -.
DR   GO; GO:0050076; F:maleate isomerase activity; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..251
FT                   /note="Maleate isomerase"
FT                   /id="PRO_0000418472"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT   BINDING         81..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT   BINDING         200..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
FT   MOD_RES         81
FT                   /note="S-(2-succinyl)cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5YXQ1"
SQ   SEQUENCE   251 AA;  27273 MW;  826707CBF5E76586 CRC64;
     MAKHFRIGMI VPSSNTTMET EIPAMLQSRM KEIPEETFTF HSSRMRMMHV TKEELKKMDE
     ESDRCAIELS DARCDVLAYA CLVAIMCQGP GYHEKSEARL ASLTAQNGGA APVISSAGAL
     IDGIRTLGAK KIALIAPYMK PLTNQVIEYI TASGIEVTDS ISLEIPDNLE VGRQDPMRLI
     EIVKNLDVSN ADAVVLSACV QMPSLPAIQK VQDQLGLPVL SAATSTVYKI LKSLNLKTYV
     PNAGSLLSGK Y