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Protein

2-methylcitrate synthase

Gene

mmgD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of citrate from acetyl-CoA and oxaloacetate. The genomic context suggests that this protein probably functions as a 2-methylcitrate synthase, i.e. catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate.1 Publication

Catalytic activityi

Propanoyl-CoA + H2O + oxaloacetate = (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.
Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei262 – 2621PROSITE-ProRule annotation
Active sitei314 – 3141PROSITE-ProRule annotation

GO - Molecular functioni

  1. 2-methylcitrate synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
  3. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU24140-MONOMER.
UniPathwayiUPA00946.

Names & Taxonomyi

Protein namesi
Recommended name:
2-methylcitrate synthase (EC:2.3.3.5)
Alternative name(s):
Citrate synthase 3 (EC:2.3.3.16)
Citrate synthase III
Methylcitrate synthase
Gene namesi
Name:mmgD
Synonyms:yqiO
Ordered Locus Names:BSU24140
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU24140. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3723722-methylcitrate synthasePRO_0000169930Add
BLAST

Proteomic databases

PaxDbiP45858.
PRIDEiP45858.

Expressioni

Developmental stagei

Expressed in the mother cell at intermediate stages of sporulation under the control of the sigma-E factor.1 Publication

Inductioni

Subject to catabolite repression.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224308.BSU24140.

Structurei

3D structure databases

ProteinModelPortaliP45858.
SMRiP45858. Positions 7-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiP45858.
KOiK01647.
OMAiHELPNST.
OrthoDBiEOG6P8TP4.
PhylomeDBiP45858.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKQHYSPG LDGVIAAETH ISYLDTQSSQ ILIRGYDLIE LSETKSYLEL
60 70 80 90 100
VHLLLEGRLP EESEMETLER KINSASSLPA DHLRLLELLP EDTHPMDGLR
110 120 130 140 150
TGLSALAGYD RQIDDRSPSA NKERAYQLLG KMPALTAASY RIINKKEPIL
160 170 180 190 200
PLQTLSYSAN FLYMMTGKLP SSLEEQIFDR SLVLYSEHEM PNSTFAARVI
210 220 230 240 250
ASTHSDLYGA LTGAVASLKG NLHGGANEAV MYLLLEAKTT SDFEQLLQTK
260 270 280 290 300
LKRKEKIMGF GHRVYMKKMD PRALMMKEAL QQLCDKAGDH RLYEMCEAGE
310 320 330 340 350
RLMEKEKGLY PNLDYYAAPV YWMLGIPIPL YTPIFFSART SGLCAHVIEQ
360 370
HANNRLFRPR VSYMGPRYQT KS
Length:372
Mass (Da):42,106
Last modified:October 31, 1995 - v1
Checksum:i29FD292E27B5F9F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29084 Genomic DNA. Translation: AAB09616.1.
D84432 Genomic DNA. Translation: BAA12590.1.
AL009126 Genomic DNA. Translation: CAB14345.1.
PIRiE69658.
RefSeqiNP_390294.1. NC_000964.3.
WP_003230298.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14345; CAB14345; BSU24140.
GeneIDi938665.
KEGGibsu:BSU24140.
PATRICi18976656. VBIBacSub10457_2518.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29084 Genomic DNA. Translation: AAB09616.1.
D84432 Genomic DNA. Translation: BAA12590.1.
AL009126 Genomic DNA. Translation: CAB14345.1.
PIRiE69658.
RefSeqiNP_390294.1. NC_000964.3.
WP_003230298.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP45858.
SMRiP45858. Positions 7-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU24140.

Proteomic databases

PaxDbiP45858.
PRIDEiP45858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14345; CAB14345; BSU24140.
GeneIDi938665.
KEGGibsu:BSU24140.
PATRICi18976656. VBIBacSub10457_2518.

Organism-specific databases

GenoListiBSU24140. [Micado]

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiP45858.
KOiK01647.
OMAiHELPNST.
OrthoDBiEOG6P8TP4.
PhylomeDBiP45858.

Enzyme and pathway databases

UniPathwayiUPA00946.
BioCyciBSUB:BSU24140-MONOMER.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A sigma E dependent operon subject to catabolite repression during sporulation in Bacillus subtilis."
    Bryan E.M., Beall B.W., Moran C.P. Jr.
    J. Bacteriol. 178:4778-4786(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A CITRATE SYNTHASE, DEVELOPMENTAL STAGE, INDUCTION.
    Strain: 168 / MB24.
  2. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
    Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
    Microbiology 142:3103-3111(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH642.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiCISY3_BACSU
AccessioniPrimary (citable) accession number: P45858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: October 31, 1995
Last modified: January 6, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.