MMGF_ALKHC
ID MMGF_ALKHC Reviewed; 300 AA.
AC Q9Z9T7; Q9JPV3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=2-methylisocitrate lyase {ECO:0000250|UniProtKB:P54528};
DE Short=2-MIC {ECO:0000250|UniProtKB:P54528};
DE Short=MICL {ECO:0000250|UniProtKB:P54528};
DE EC=4.1.3.- {ECO:0000250|UniProtKB:P54528};
GN Name=mmgF {ECO:0000250|UniProtKB:P54528}; OrderedLocusNames=BH3922;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=10086842; DOI=10.1007/s007920050096;
RA Takami H., Nakasone K., Ogasawara N., Hirama C., Nakamura Y., Masui N.,
RA Fuji F., Takaki Y., Inoue A., Horikoshi K.;
RT "Sequencing of three lambda clones from the genome of alkaliphilic Bacillus
RT sp. strain C-125.";
RL Extremophiles 3:29-34(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Involved in the methylcitric acid cycle. Catalyzes the
CC cleavage of 2-methylisocitrate to yield pyruvate and succinate.
CC {ECO:0000250|UniProtKB:P54528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate;
CC Xref=Rhea:RHEA:57504, ChEBI:CHEBI:15361, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:141790; Evidence={ECO:0000250|UniProtKB:P54528};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P77541};
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000305}.
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DR EMBL; AB011838; BAA75345.1; -; Genomic_DNA.
DR EMBL; BA000004; BAB07641.1; -; Genomic_DNA.
DR PIR; B84140; B84140.
DR RefSeq; WP_010900047.1; NC_002570.2.
DR AlphaFoldDB; Q9Z9T7; -.
DR SMR; Q9Z9T7; -.
DR STRING; 272558.10176547; -.
DR PRIDE; Q9Z9T7; -.
DR EnsemblBacteria; BAB07641; BAB07641; BAB07641.
DR KEGG; bha:BH3922; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_9; -.
DR OMA; QTELWNK; -.
DR OrthoDB; 1485205at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:InterPro.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR012695; PrpB.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR02317; prpB; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..300
FT /note="2-methylisocitrate lyase"
FT /id="PRO_0000068819"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 129..130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
SQ SEQUENCE 300 AA; 32612 MW; D927DA47AD3FAD5D CRC64;
MAWIVEQPKS QKELADRFRQ LMKEEAILQI PGAHDAMAAL VAKKAGFSAL YLSGDAYTAS
RGLPDLGIVT STEVADRAKD LVRATNLPVL VDIDTGFGGV LNVARTAQEM LEANVAAVQI
EDQQLPKKCG HLNGKQLVSK EEMEQKIQAI KKVAPTLVIV ARTDARANEG LNGAIERANV
YIEAGADAIF PEALQSAEEF RLVAENVSAP LLANMTEFGK TPLMTAGGLQ NAGFQMVIYP
VTSLRVAAKA YERIFQLIKD EGTQEAGIED MQTRKELYET ISYDDFEALD KNIAKTVLGE
