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P39119

- CISY_BACSU

UniProt

P39119 - CISY_BACSU

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Protein
Citrate synthase 1
Gene
citA, BSU09440
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei252 – 2521 By similarity
Active sitei307 – 3071 By similarity

GO - Molecular functioni

  1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer Source: InterPro

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciBSUB:BSU09440-MONOMER.
RETL1328306-WGS:GSTH-2193-MONOMER.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase 1 (EC:2.3.3.16)
Alternative name(s):
Citrate synthase I
Gene namesi
Name:citA
Ordered Locus Names:BSU09440
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU09440. [Micado]

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3071E → D: 5-fold increase in activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Citrate synthase 1
PRO_0000169928Add
BLAST

Proteomic databases

PaxDbiP39119.
PRIDEiP39119.

Expressioni

Inductioni

By decoyinine and nutrient depletion.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

STRINGi224308.BSU09440.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63
Beta strandi12 – 209
Turni21 – 244
Beta strandi25 – 284
Helixi33 – 397
Helixi42 – 5110
Helixi57 – 7014
Helixi75 – 839
Beta strandi86 – 883
Helixi90 – 10112
Helixi112 – 13322
Helixi148 – 1569
Helixi162 – 17615
Helixi182 – 19110
Turni192 – 1943
Helixi197 – 20913
Helixi218 – 2258
Helixi233 – 24210
Helixi260 – 27112
Turni272 – 2743
Helixi277 – 29620
Helixi307 – 31610
Helixi321 – 3233
Helixi324 – 34320
Turni344 – 3463
Beta strandi353 – 3564

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C6XX-ray3.40A/B/C/D2-364[»]
ProteinModelPortaliP39119.
SMRiP39119. Positions 2-364.

Miscellaneous databases

EvolutionaryTraceiP39119.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
KOiK01647.
OrthoDBiEOG6P8TP4.
PhylomeDBiP39119.

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.

P39119-1 [UniParc]FASTAAdd to Basket

« Hide

MVHYGLKGIT CVETSISHID GEKGRLIYRG HHAKDIALNH SFEEAAYLIL    50
FGKLPSTEEL QVFKDKLAAE RNLPEHIERL IQSLPNNMDD MSVLRTVVSA 100
LGENTYTFHP KTEEAIRLIA ITPSIIAYRK RWTRGEQAIA PSSQYGHVEN 150
YYYMLTGEQP SEAKKKALET YMILATEHGM NASTFSARVT LSTESDLVSA 200
VTAALGTMKG PLHGGAPSAV TKMLEDIGEK EHAEAYLKEK LEKGERLMGF 250
GHRVYKTKDP RAEALRQKAE EVAGNDRDLD LALHVEAEAI RLLEIYKPGR 300
KLYTNVEFYA AAVMRAIDFD DELFTPTFSA SRMVGWCAHV LEQAENNMIF 350
RPSAQYTGAI PEEVLS 366
Length:366
Mass (Da):40,952
Last modified:June 16, 2009 - v2
Checksum:iADF8AB7CFE837861
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → V in AAA20936. 1 Publication
Sequence conflicti94 – 941L → V in CAA74489. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05256 Genomic DNA. Translation: AAA20936.1.
Y14082 Genomic DNA. Translation: CAA74489.1.
AL009126 Genomic DNA. Translation: CAB12783.2.
PIRiI40380.
RefSeqiNP_388825.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12783; CAB12783; BSU09440.
GeneIDi936270.
KEGGibsu:BSU09440.
PATRICi18973584. VBIBacSub10457_0986.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05256 Genomic DNA. Translation: AAA20936.1 .
Y14082 Genomic DNA. Translation: CAA74489.1 .
AL009126 Genomic DNA. Translation: CAB12783.2 .
PIRi I40380.
RefSeqi NP_388825.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C6X X-ray 3.40 A/B/C/D 2-364 [» ]
ProteinModelPortali P39119.
SMRi P39119. Positions 2-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU09440.

Proteomic databases

PaxDbi P39119.
PRIDEi P39119.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12783 ; CAB12783 ; BSU09440 .
GeneIDi 936270.
KEGGi bsu:BSU09440.
PATRICi 18973584. VBIBacSub10457_0986.

Organism-specific databases

GenoListi BSU09440. [Micado ]

Phylogenomic databases

eggNOGi COG0372.
HOGENOMi HOG000021225.
KOi K01647.
OrthoDBi EOG6P8TP4.
PhylomeDBi P39119.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .
BioCyci BSUB:BSU09440-MONOMER.
RETL1328306-WGS:GSTH-2193-MONOMER.

Miscellaneous databases

EvolutionaryTracei P39119.

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. "Identification of two distinct Bacillus subtilis citrate synthase genes."
    Jin S., Sonenshein A.L.
    J. Bacteriol. 176:4669-4679(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / SMY.
  2. "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
    Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
    Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  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.
  4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 94.

Entry informationi

Entry nameiCISY_BACSU
AccessioniPrimary (citable) accession number: P39119
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.

Keywords - Technical termi

3D-structure, Allosteric enzyme, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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