(data stored in SCRATCH zone)

SWISSPROT: MMGE_BACSU

ID   MMGE_BACSU              Reviewed;         472 AA.
AC   P45859;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=Citrate/2-methylcitrate dehydratase {ECO:0000303|PubMed:28956599};
DE            EC=4.2.1.- {ECO:0000269|PubMed:28956599};
GN   Name=mmgE {ECO:0000303|PubMed:8759838}; Synonyms=prpD, yqiP;
GN   OrderedLocusNames=BSU24130;
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   SEQUENCE REVISION TO 216.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RC   STRAIN=168 / MB24;
RX   PubMed=8759838; DOI=10.1128/jb.178.16.4778-4786.1996;
RA   Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT   "A sigma E dependent operon subject to catabolite repression during
RT   sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 178:4778-4786(1996).
RN   [5]
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).
RN   [6] {ECO:0000244|PDB:5MUX}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RA   Baker G.E., Race P.R.;
RT   "Crystal structure of 2-methylcitrate dehydratase (MmgE) from Bacillus
RT   subtilis.";
RL   Submitted (JAN-2017) to the PDB data bank.
CC   -!- FUNCTION: Involved in both the tricarboxylic acid (TCA) and
CC       methylcitric acid cycles (PubMed:28956599). Has both 2-methylcitrate
CC       dehydratase and citrate dehydratase activities. Catalyzes the
CC       dehydration of 2-methylcitrate (2-MC) to yield 2-methyl-cis-aconitate,
CC       and the dehydration of citrate to yield cis-aconitate. Cannot form
CC       isocitrate. Uses either (2S,3R)- or (2R,3S)-2-methylcitrate
CC       (PubMed:28956599). {ECO:0000269|PubMed:28956599}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylcitrate = 2-methyl-cis-aconitate + H2O;
CC         Xref=Rhea:RHEA:57496, ChEBI:CHEBI:15377, ChEBI:CHEBI:15598,
CC         ChEBI:CHEBI:57872; Evidence={ECO:0000269|PubMed:28956599};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = cis-aconitate + H2O; Xref=Rhea:RHEA:10228,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16383, ChEBI:CHEBI:16947;
CC         Evidence={ECO:0000269|PubMed:28956599};
CC   -!- DEVELOPMENTAL STAGE: Expressed in the mother cell at intermediate
CC       stages of sporulation under the control of the sigma-E factor.
CC       {ECO:0000269|PubMed:8759838}.
CC   -!- INDUCTION: Subject to catabolite repression.
CC       {ECO:0000269|PubMed:8759838}.
CC   -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
DR   EMBL; D84432; BAA12591.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14344.2; -; Genomic_DNA.
DR   EMBL; U29084; AAB09617.1; -; Genomic_DNA.
DR   PIR; F69658; F69658.
DR   RefSeq; NP_390293.2; NC_000964.3.
DR   RefSeq; WP_004398686.1; NZ_JNCM01000036.1.
DR   PDB; 5MUX; X-ray; 2.00 A; A/B/C/D/E/F=1-472.
DR   PDBsum; 5MUX; -.
DR   SMR; P45859; -.
DR   STRING; 224308.BSU24130; -.
DR   PaxDb; P45859; -.
DR   PRIDE; P45859; -.
DR   EnsemblBacteria; CAB14344; CAB14344; BSU24130.
DR   GeneID; 938663; -.
DR   KEGG; bsu:BSU24130; -.
DR   PATRIC; fig|224308.43.peg.2517; -.
DR   eggNOG; ENOG4105DXD; Bacteria.
DR   eggNOG; COG2079; LUCA.
DR   HOGENOM; HOG000159916; -.
DR   InParanoid; P45859; -.
DR   KO; K01720; -.
DR   OMA; ECTKHLG; -.
DR   PhylomeDB; P45859; -.
DR   BioCyc; BSUB:BSU24130-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0047547; F:2-methylcitrate dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.4100.10; -; 1.
DR   Gene3D; 3.30.1330.120; -; 1.
DR   InterPro; IPR012705; 2Me_IsoCit_deHydtase_PrpD.
DR   InterPro; IPR036148; MmgE/PrpD_sf.
DR   InterPro; IPR042183; MmgE/PrpD_sf_1.
DR   InterPro; IPR042188; MmgE/PrpD_sf_2.
DR   InterPro; IPR005656; MmgE_PrpD.
DR   PANTHER; PTHR16943; PTHR16943; 1.
DR   Pfam; PF03972; MmgE_PrpD; 1.
DR   SUPFAM; SSF103378; SSF103378; 1.
DR   TIGRFAMs; TIGR02330; prpD; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P45859.
DR   SWISS-2DPAGE; P45859.
KW   3D-structure; Lyase; Reference proteome; Sporulation;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..472
FT                   /note="Citrate/2-methylcitrate dehydratase"
FT                   /id="PRO_0000215020"
FT   CONFLICT        216
FT                   /note="A -> P (in Ref. 1; BAA12591)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..17
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           23..43
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           47..50
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           77..89
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   STRAND          96..103
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           105..108
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           109..125
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           133..153
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           157..159
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           164..178
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           183..195
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           202..204
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   TURN            206..208
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           211..213
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           216..232
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   TURN            239..243
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   TURN            245..247
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           249..253
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   STRAND          265..267
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           268..271
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           283..285
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           286..299
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   STRAND          308..313
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           315..320
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           330..334
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           337..347
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           352..355
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           357..360
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           363..369
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   STRAND          372..376
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           378..385
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   TURN            387..389
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   STRAND          394..399
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   STRAND          409..413
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           418..420
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           421..437
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           442..453
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           455..458
FT                   /evidence="ECO:0000244|PDB:5MUX"
FT   HELIX           463..466
FT                   /evidence="ECO:0000244|PDB:5MUX"
SQ   SEQUENCE   472 AA;  52878 MW;  5941EA6EC1DA2142 CRC64;
     MPKTDRVIEE ITDYVLEKEI TSAEAYTTAG HVLLDTLGCG ILALRYPECT KLLGPIVPGT
     TVPNGSKVPG TSYVLDPVRA AFNIGCMIRW LDYNDTWLAA EWGHPSDNLG GILAAADYVS
     RVRLSEGKEP LTVRDVLEMM IKAHEIQGVL ALENSLNRVG LDHVLFVKVA TTAVAAKLLG
     GGREEIKNAL SNAWIDNAAL RTYRHSPNTG SRKSWAAGDA TSRGVHLALM SLKGEMGYPT
     ALSAPGWGFQ DVLFNKKEIK LARPLDAYVM ENVLFKVSYP AEFHAQTAAE SAVILHPQVK
     NRIDEIDRVV IRTHESAIRI IDKKGPLHNP ADRDHCLQYI TAIGLLFGDI TAQHYEAETA
     NDPRIDKLRD KMEVTENKTY TEDYLKPDKR SISNAVQVHF KDGTSTEMVE CEFPLGHRFR
     REEAVPKLLE KFSDNLKTHF PDKQHKHIYE RCTSYETLQT MRVNEFVDMF CM
//

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