MMGF_BACSU
ID MMGF_BACSU Reviewed; 301 AA.
AC P54528;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=2-methylisocitrate lyase {ECO:0000303|PubMed:28956599};
DE Short=2-MIC {ECO:0000305};
DE Short=MICL {ECO:0000305};
DE EC=4.1.3.- {ECO:0000269|PubMed:28956599};
GN Name=mmgF {ECO:0000303|PubMed:28956599}; Synonyms=prpB, yqiQ;
GN OrderedLocusNames=BSU24120;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=168;
RX PubMed=28956599; DOI=10.1021/acs.biochem.7b00778;
RA Reddick J.J., Sirkisoon S., Dahal R.A., Hardesty G., Hage N.E., Booth W.T.,
RA Quattlebaum A.L., Mills S.N., Meadows V.G., Adams S.L.H., Doyle J.S.,
RA Kiel B.E.;
RT "First biochemical characterization of a methylcitric acid cycle from
RT Bacillus subtilis strain 168.";
RL Biochemistry 56:5698-5711(2017).
CC -!- FUNCTION: Involved in the methylcitric acid cycle. Catalyzes the
CC cleavage of 2-methylisocitrate to yield pyruvate and succinate.
CC {ECO:0000269|PubMed:28956599}.
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:0000269|PubMed:28956599};
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; D84432; BAA12592.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14343.1; -; Genomic_DNA.
DR PIR; G69961; G69961.
DR RefSeq; NP_390292.1; NC_000964.3.
DR RefSeq; WP_004398772.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54528; -.
DR SMR; P54528; -.
DR STRING; 224308.BSU24120; -.
DR PaxDb; P54528; -.
DR PRIDE; P54528; -.
DR EnsemblBacteria; CAB14343; CAB14343; BSU_24120.
DR GeneID; 938668; -.
DR KEGG; bsu:BSU24120; -.
DR PATRIC; fig|224308.179.peg.2626; -.
DR eggNOG; COG2513; Bacteria.
DR InParanoid; P54528; -.
DR OMA; QTELWNK; -.
DR PhylomeDB; P54528; -.
DR BioCyc; BSUB:BSU24120-MON; -.
DR BRENDA; 4.1.3.30; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IBA:GO_Central.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IBA:GO_Central.
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 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..301
FT /note="2-methylisocitrate lyase"
FT /id="PRO_0000068820"
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 301 AA; 33097 MW; DAA867684727A942 CRC64;
MSWIVNKQSS QEELAGRFRK LMSAPDILQI PGAHDGMAAL LAKEAGFSAI YLSGAAYTAS
RGLPDLGIIT SAEIAERAKD LVRAADLPLL VDIDTGFGGV LNAARTAREM LEARVAAVQM
EDQQLPKKCG HLNGKQLVPI KEMAQKIKAI KQAAPSLIVV ARTDARAQEG LDAAIKRSEA
YIEAGADAIF PEALQAENEF RQFAERIPVP LLANMTEFGK TPYYRADEFE DMGFHMVIYP
VTSLRAAAKA CERMFGLMKE HGSQKEGLHD MQTRKELYDT ISYYDYEALD KTIAKTVLPD
E
