(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 122.
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}.
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   SMR; P54528; -.
DR   STRING; 224308.BSU24120; -.
DR   PaxDb; P54528; -.
DR   PRIDE; P54528; -.
DR   EnsemblBacteria; CAB14343; CAB14343; BSU24120.
DR   GeneID; 938668; -.
DR   KEGG; bsu:BSU24120; -.
DR   PATRIC; fig|224308.179.peg.2626; -.
DR   eggNOG; ENOG4105CR4; Bacteria.
DR   eggNOG; COG2513; LUCA.
DR   HOGENOM; HOG000220041; -.
DR   InParanoid; P54528; -.
DR   KO; K03417; -.
DR   OMA; SMVLYPL; -.
DR   PhylomeDB; P54528; -.
DR   BioCyc; BSUB:BSU24120-MONOMER; -.
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;
DR   PRODOM; P54528.
DR   SWISS-2DPAGE; P54528.
KW   Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..301
FT                   /note="2-methylisocitrate lyase"
FT                   /id="PRO_0000068820"
FT   REGION          53..55
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P77541"
FT   REGION          129..130
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P77541"
FT   REGION          214..216
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P77541"
FT   METAL           92
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P77541"
FT   METAL           94
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P77541"
FT   BINDING         162
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P77541"
FT   BINDING         192
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P77541"
FT   BINDING         245
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P77541"
FT   BINDING         274
FT                   /note="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
//

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