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Protein

Citrate synthase 1

Gene

citA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Pathway:itricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes isocitrate from oxaloacetate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase 2 (citZ), Citrate synthase 1 (citA)
  2. Aconitate hydratase A (citB), 2-methylcitrate dehydratase (prpD), 2-methylcitrate synthase (mmgD)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei252 – 2521PROSITE-ProRule annotation
Active sitei307 – 3071PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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 Componenti: 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 1PRO_0000169928Add
BLAST

Proteomic databases

PaxDbiP39119.
PRIDEiP39119.

Expressioni

Inductioni

By decoyinine and nutrient depletion.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005286.

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi12 – 209Combined sources
Turni21 – 244Combined sources
Beta strandi25 – 284Combined sources
Helixi33 – 397Combined sources
Helixi42 – 5110Combined sources
Helixi57 – 7014Combined sources
Helixi75 – 839Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 10112Combined sources
Helixi112 – 13322Combined sources
Helixi148 – 1569Combined sources
Helixi162 – 17615Combined sources
Helixi182 – 19110Combined sources
Turni192 – 1943Combined sources
Helixi197 – 20913Combined sources
Helixi218 – 2258Combined sources
Helixi233 – 24210Combined sources
Helixi260 – 27112Combined sources
Turni272 – 2743Combined sources
Helixi277 – 29620Combined sources
Helixi307 – 31610Combined sources
Helixi321 – 3233Combined sources
Helixi324 – 34320Combined sources
Turni344 – 3463Combined sources
Beta strandi353 – 3564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C6XX-ray3.40A/B/C/D2-364[»]
ProteinModelPortaliP39119.
SMRiP39119. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39119.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiP39119.
KOiK01647.
OMAiGLKGITC.
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.
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

        10         20         30         40         50
MVHYGLKGIT CVETSISHID GEKGRLIYRG HHAKDIALNH SFEEAAYLIL
60 70 80 90 100
FGKLPSTEEL QVFKDKLAAE RNLPEHIERL IQSLPNNMDD MSVLRTVVSA
110 120 130 140 150
LGENTYTFHP KTEEAIRLIA ITPSIIAYRK RWTRGEQAIA PSSQYGHVEN
160 170 180 190 200
YYYMLTGEQP SEAKKKALET YMILATEHGM NASTFSARVT LSTESDLVSA
210 220 230 240 250
VTAALGTMKG PLHGGAPSAV TKMLEDIGEK EHAEAYLKEK LEKGERLMGF
260 270 280 290 300
GHRVYKTKDP RAEALRQKAE EVAGNDRDLD LALHVEAEAI RLLEIYKPGR
310 320 330 340 350
KLYTNVEFYA AAVMRAIDFD DELFTPTFSA SRMVGWCAHV LEQAENNMIF
360
RPSAQYTGAI PEEVLS
Length:366
Mass (Da):40,952
Last modified:June 16, 2009 - v2
Checksum:iADF8AB7CFE837861
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → V in AAA20936 (PubMed:8045898).Curated
Sequence conflicti94 – 941L → V in CAA74489 (PubMed:9579061).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_003244745.1. NZ_JNCM01000035.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_003244745.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C6XX-ray3.40A/B/C/D2-364[»]
ProteinModelPortaliP39119.
SMRiP39119. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005286.

Proteomic databases

PaxDbiP39119.
PRIDEiP39119.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU09440. [Micado]

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiP39119.
KOiK01647.
OMAiGLKGITC.
OrthoDBiEOG6P8TP4.
PhylomeDBiP39119.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP39119.

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.
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. "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 22, 2015
This is version 113 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

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.