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P45858 (CISY3_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-methylcitrate synthase

EC=2.3.3.5
Alternative name(s):
Citrate synthase 3
EC=2.3.3.1
Citrate synthase III
Methylcitrate synthase
Gene names
Name:mmgD
Synonyms:yqiO
Ordered Locus Names:BSU24140
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

Propanoyl-CoA + H2O + oxaloacetate = (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Pathway

Organic acid metabolism; propanoate degradation.

Subunit structure

Homodimer By similarity.

Developmental stage

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

Induction

Subject to catabolite repression. Ref.1

Sequence similarities

Belongs to the citrate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3723722-methylcitrate synthase
PRO_0000169930

Sites

Active site2621 By similarity
Active site3141 By similarity

Sequences

Sequence LengthMass (Da)Tools
P45858 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 29FD292E27B5F9F7

FASTA37242,106
        10         20         30         40         50         60 
MEEKQHYSPG LDGVIAAETH ISYLDTQSSQ ILIRGYDLIE LSETKSYLEL VHLLLEGRLP 

        70         80         90        100        110        120 
EESEMETLER KINSASSLPA DHLRLLELLP EDTHPMDGLR TGLSALAGYD RQIDDRSPSA 

       130        140        150        160        170        180 
NKERAYQLLG KMPALTAASY RIINKKEPIL PLQTLSYSAN FLYMMTGKLP SSLEEQIFDR 

       190        200        210        220        230        240 
SLVLYSEHEM PNSTFAARVI ASTHSDLYGA LTGAVASLKG NLHGGANEAV MYLLLEAKTT 

       250        260        270        280        290        300 
SDFEQLLQTK LKRKEKIMGF GHRVYMKKMD PRALMMKEAL QQLCDKAGDH RLYEMCEAGE 

       310        320        330        340        350        360 
RLMEKEKGLY PNLDYYAAPV YWMLGIPIPL YTPIFFSART SGLCAHVIEQ HANNRLFRPR 

       370 
VSYMGPRYQT KS 

« Hide

References

« Hide 'large scale' references
[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(1996) [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(1996) [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. expand/collapse author list , 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(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29084 Genomic DNA. Translation: AAB09616.1.
D84432 Genomic DNA. Translation: BAA12590.1.
AL009126 Genomic DNA. Translation: CAB14345.1.
PIRE69658.
RefSeqNP_390294.1. NC_000964.3.

3D structure databases

ProteinModelPortalP45858.
SMRP45858. Positions 7-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU24140.

Proteomic databases

PaxDbP45858.
PRIDEP45858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14345; CAB14345; BSU24140.
GeneID938665.
KEGGbsu:BSU24140.
PATRIC18976656. VBIBacSub10457_2518.

Organism-specific databases

GenoListBSU24140. [Micado]

Phylogenomic databases

eggNOGCOG0372.
HOGENOMHOG000021225.
KOK01647.
OMAKGNLHGG.
OrthoDBEOG6P8TP4.
ProtClustDBPRK12349.

Enzyme and pathway databases

BioCycBSUB:BSU24140-MONOMER.
UniPathwayUPA00946.

Family and domain databases

Gene3D1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProIPR016142. 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]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFPIRSF001369. Citrate_synth. 1 hit.
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCISY3_BACSU
AccessionPrimary (citable) accession number: P45858
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 13, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList