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 03-AUG-2022, entry version 130.
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:0007744|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}.
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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 AlphaFoldDB; P45859; -.
DR SMR; P45859; -.
DR STRING; 224308.BSU24130; -.
DR PaxDb; P45859; -.
DR PRIDE; P45859; -.
DR EnsemblBacteria; CAB14344; CAB14344; BSU_24130.
DR GeneID; 938663; -.
DR KEGG; bsu:BSU24130; -.
DR PATRIC; fig|224308.43.peg.2517; -.
DR eggNOG; COG2079; Bacteria.
DR InParanoid; P45859; -.
DR OMA; ECTKHLG; -.
DR PhylomeDB; P45859; -.
DR BioCyc; BSUB:BSU24130-MON; -.
DR BRENDA; 4.2.1.79; 658.
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:0047780; F:citrate dehydratase activity; IEA:RHEA.
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 InterPro; IPR045337; MmgE_PrpD_C.
DR InterPro; IPR045336; MmgE_PrpD_N.
DR PANTHER; PTHR16943; PTHR16943; 1.
DR Pfam; PF03972; MmgE_PrpD; 1.
DR Pfam; PF19305; MmgE_PrpD_C; 1.
DR SUPFAM; SSF103378; SSF103378; 1.
DR TIGRFAMs; TIGR02330; prpD; 1.
PE 1: Evidence at protein level;
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:0007829|PDB:5MUX"
FT HELIX 23..43
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:5MUX"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 133..153
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5MUX"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:5MUX"
FT TURN 239..243
FT /evidence="ECO:0007829|PDB:5MUX"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:5MUX"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:5MUX"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 337..347
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:5MUX"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:5MUX"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:5MUX"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:5MUX"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 421..437
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 442..453
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:5MUX"
FT HELIX 463..466
FT /evidence="ECO:0007829|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
