SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P45858

- CISY3_BACSU

UniProt

P45858 - CISY3_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
2-methylcitrate synthase
Gene
mmgD, yqiO, BSU24140
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei262 – 2621 By similarity
Active sitei314 – 3141 By similarity

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: Chromosome

Organism-specific databases

GenoListiBSU24140. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3723722-methylcitrate synthase
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
KOiK01647.
OMAiFANTAGC.
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

MEEKQHYSPG LDGVIAAETH ISYLDTQSSQ ILIRGYDLIE LSETKSYLEL    50
VHLLLEGRLP EESEMETLER KINSASSLPA DHLRLLELLP EDTHPMDGLR 100
TGLSALAGYD RQIDDRSPSA NKERAYQLLG KMPALTAASY RIINKKEPIL 150
PLQTLSYSAN FLYMMTGKLP SSLEEQIFDR SLVLYSEHEM PNSTFAARVI 200
ASTHSDLYGA LTGAVASLKG NLHGGANEAV MYLLLEAKTT SDFEQLLQTK 250
LKRKEKIMGF GHRVYMKKMD PRALMMKEAL QQLCDKAGDH RLYEMCEAGE 300
RLMEKEKGLY PNLDYYAAPV YWMLGIPIPL YTPIFFSART SGLCAHVIEQ 350
HANNRLFRPR VSYMGPRYQT KS 372
Length:372
Mass (Da):42,106
Last modified:November 1, 1995 - v1
Checksum:i29FD292E27B5F9F7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29084 Genomic DNA. Translation: AAB09616.1 .
D84432 Genomic DNA. Translation: BAA12590.1 .
AL009126 Genomic DNA. Translation: CAB14345.1 .
PIRi E69658.
RefSeqi NP_390294.1. NC_000964.3.
WP_003230298.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali P45858.
SMRi P45858. Positions 7-372.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU24140.

Proteomic databases

PaxDbi P45858.
PRIDEi P45858.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14345 ; CAB14345 ; BSU24140 .
GeneIDi 938665.
KEGGi bsu:BSU24140.
PATRICi 18976656. VBIBacSub10457_2518.

Organism-specific databases

GenoListi BSU24140. [Micado ]

Phylogenomic databases

eggNOGi COG0372.
HOGENOMi HOG000021225.
KOi K01647.
OMAi FANTAGC.
OrthoDBi EOG6P8TP4.
PhylomeDBi P45858.

Enzyme and pathway databases

UniPathwayi UPA00946 .
BioCyci BSUB:BSU24140-MONOMER.

Family and domain databases

Gene3Di 1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProi IPR016142. 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 ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PIRSFi PIRSF001369. Citrate_synth. 1 hit.
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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.

Entry informationi

Entry nameiCISY3_BACSU
AccessioniPrimary (citable) accession number: P45858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 109 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