Skip Header

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

Pathwayi: tricarboxylic 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)DescriptionActionsGraphical viewLength
Active sitei252PROSITE-ProRule annotation1
Active sitei307PROSITE-ProRule annotation1

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.
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
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi307E → D: 5-fold increase in activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001699281 – 366Citrate synthase 1Add BLAST366

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

1366
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi12 – 20Combined sources9
Turni21 – 24Combined sources4
Beta strandi25 – 28Combined sources4
Helixi33 – 39Combined sources7
Helixi42 – 51Combined sources10
Helixi57 – 70Combined sources14
Helixi75 – 83Combined sources9
Beta strandi86 – 88Combined sources3
Helixi90 – 101Combined sources12
Helixi112 – 133Combined sources22
Helixi148 – 156Combined sources9
Helixi162 – 176Combined sources15
Helixi182 – 191Combined sources10
Turni192 – 194Combined sources3
Helixi197 – 209Combined sources13
Helixi218 – 225Combined sources8
Helixi233 – 242Combined sources10
Helixi260 – 271Combined sources12
Turni272 – 274Combined sources3
Helixi277 – 296Combined sources20
Helixi307 – 316Combined sources10
Helixi321 – 323Combined sources3
Helixi324 – 343Combined sources20
Turni344 – 346Combined sources3
Beta strandi353 – 356Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP39119.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105BZN. Bacteria.
COG0372. LUCA.
HOGENOMiHOG000021225.
InParanoidiP39119.
KOiK01647.
OMAiHHAKDIA.
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)DescriptionActionsGraphical viewLength
Sequence conflicti94L → V in AAA20936 (PubMed:8045898).Curated1
Sequence conflicti94L → V in CAA74489 (PubMed:9579061).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C6XX-ray3.40A/B/C/D2-364[»]
ProteinModelPortaliP39119.
SMRiP39119.
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.

Phylogenomic databases

eggNOGiENOG4105BZN. Bacteria.
COG0372. LUCA.
HOGENOMiHOG000021225.
InParanoidiP39119.
KOiK01647.
OMAiHHAKDIA.
PhylomeDBiP39119.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciBSUB:BSU09440-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...

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: November 2, 2016
This is version 121 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

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 one 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.