MAIA_NOCFA
ID MAIA_NOCFA Reviewed; 251 AA.
AC Q5YXQ1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Maleate isomerase {ECO:0000255|HAMAP-Rule:MF_00943, ECO:0000303|PubMed:20677745};
DE Short=MI {ECO:0000303|PubMed:20677745};
DE EC=5.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00943, ECO:0000269|PubMed:20677745};
DE AltName: Full=Maleate cis-trans isomerase {ECO:0000255|HAMAP-Rule:MF_00943};
GN Name=maiA {ECO:0000255|HAMAP-Rule:MF_00943};
GN OrderedLocusNames=NFA_21930 {ECO:0000312|EMBL:BAD57040.1};
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
RN [2] {ECO:0007744|PDB:2XEC, ECO:0007744|PDB:2XED}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH
RP A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT,
RP REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, AND MUTAGENESIS OF
RP CYS-76; TYR-133 AND CYS-194.
RC STRAIN=IFM 10152;
RX PubMed=20677745; DOI=10.1021/ja1053576;
RA Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B.,
RA Turkenburg J.P., Hart S., Bruce N.C., Grogan G.;
RT "A covalent succinylcysteine-like intermediate in the enzyme-catalyzed
RT transformation of maleate to fumarate by maleate isomerase.";
RL J. Am. Chem. Soc. 132:11455-11457(2010).
CC -!- FUNCTION: Catalyzes cis-trans isomerization of the C2-C3 double bond in
CC maleate to yield fumarate. Shows a strict specificity for maleate, with
CC no activity detected toward structurally related substrates including
CC citraconate, mesaconate, dimethylmaleate, and maleamide.
CC {ECO:0000269|PubMed:20677745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=maleate = fumarate; Xref=Rhea:RHEA:13169, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30780; EC=5.2.1.1;
CC Evidence={ECO:0000269|PubMed:20677745};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 uM for maleate (at pH 7.5) {ECO:0000269|PubMed:20677745};
CC Note=kcat is 2.8 sec(-1). {ECO:0000269|PubMed:20677745};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:20677745};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20677745}.
CC -!- MISCELLANEOUS: Reaction is initiated by nucleophilic attack of cysteine
CC at the double bond, yielding a covalent succinylcysteine-like
CC intermediate. {ECO:0000269|PubMed:20677745}.
CC -!- SIMILARITY: Belongs to the maleate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00943}.
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DR EMBL; AP006618; BAD57040.1; -; Genomic_DNA.
DR RefSeq; WP_011208725.1; NC_006361.1.
DR PDB; 2XEC; X-ray; 2.20 A; A/B/C/D=1-251.
DR PDB; 2XED; X-ray; 1.95 A; A/B/C/D=1-251.
DR PDBsum; 2XEC; -.
DR PDBsum; 2XED; -.
DR AlphaFoldDB; Q5YXQ1; -.
DR SMR; Q5YXQ1; -.
DR STRING; 247156.NFA_21930; -.
DR EnsemblBacteria; BAD57040; BAD57040; NFA_21930.
DR GeneID; 61132954; -.
DR KEGG; nfa:NFA_21930; -.
DR eggNOG; COG3473; Bacteria.
DR HOGENOM; CLU_068086_0_0_11; -.
DR OMA; DADSDRC; -.
DR BioCyc; NFAR247156:NFA_RS11020-MON; -.
DR BRENDA; 5.2.1.1; 10091.
DR EvolutionaryTrace; Q5YXQ1; -.
DR Proteomes; UP000006820; Chromosome.
DR GO; GO:0050076; F:maleate isomerase activity; IEA:UniProtKB-UniRule.
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 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..251
FT /note="Maleate isomerase"
FT /id="PRO_0000448066"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:20677745"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:20677745"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20677745"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20677745"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20677745"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20677745"
FT BINDING 195..196
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20677745"
FT MOD_RES 76
FT /note="S-(2-succinyl)cysteine"
FT /evidence="ECO:0000269|PubMed:20677745,
FT ECO:0007744|PDB:2XED"
FT MUTAGEN 76
FT /note="C->S: Reduces catalytic activity by more than 1000-
FT fold. No change in substrate affinity."
FT /evidence="ECO:0000269|PubMed:20677745"
FT MUTAGEN 133
FT /note="Y->F: No change in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20677745"
FT MUTAGEN 194
FT /note="C->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:20677745"
FT MUTAGEN 194
FT /note="C->S: Reduces catalytic activity by more than 1000-
FT fold. No change in substrate affinity."
FT /evidence="ECO:0000269|PubMed:20677745"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:2XED"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:2XED"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:2XED"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2XED"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:2XED"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:2XED"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:2XED"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2XED"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:2XED"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2XEC"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:2XED"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:2XED"
SQ SEQUENCE 251 AA; 26457 MW; 4381DC35CDC54FFB CRC64;
MGIRRIGLVV PSSNVTVETE MPALLSRHPG AEFSFHSTRM RMHTVSPEGL AAMNAQRERC
VLEIADAAPE VILYACLVAV MVGGPGEHHR VESAVAEQLA TGGSQALVRS SAGALVEGLR
ALDAQRVALV TPYMRPLAEK VVAYLEAEGF TISDWRALEV ADNTEVGCIP GEQVMAAARS
LDLSEVDALV ISCCVQMPSL PLVETAEREF GIPVLSAATA GAYSILRSLD LPVAVPGAGR
LLRQDSAVTA S
