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O34002 (CISY_ABDS2) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 70. 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:
Citrate synthase

EC=2.3.3.1
Gene names
Name:gltA
Synonyms:cisY
OrganismAntarctic bacterium DS2-3R
Taxonomic identifier56673 [NCBI]
Taxonomic lineageBacteria

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.

Subunit structure

Homodimer.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 31 degrees Celsius. Cold-active. Is rapidly inactivated at 45 degrees Celsius, and shows significant activity at 10 degrees Celsius and below.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Molecular functionTransferase
   Technical term3D-structure
Allosteric enzyme
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncitrate (Si)-synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Citrate synthase
PRO_0000169925

Sites

Active site2701 By similarity
Active site3211 By similarity

Secondary structure

............................................ 379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34002 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7D8F4614E3D1CC9F

FASTA37941,832
        10         20         30         40         50         60 
MTEPTIHKGL AGVTADVTAI SKVNSDTNSL LYRGYPVQEL AAKCSFEQVA YLLWNSELPN 

        70         80         90        100        110        120 
DSELKAFVNF ERSHRKLDEN VKGAIDLLST ACHPMDVART AVSVLGANHA RAQDSSPEAN 

       130        140        150        160        170        180 
LEKAMSLLAT FPSVVAYDQR RRRGEELIEP REDLDYSANF LWMTFGEEAA PEVVEAFNVS 

       190        200        210        220        230        240 
MILYAEHSFN ASTFTARVIT STLADLHSAV TGAIGALKGP LHGGANEAVM HTFEEIGIRK 

       250        260        270        280        290        300 
DESLDEAATR SKAWMVDALA QKKKVMGFGH RVYKNGDSRV PTMKSALDAM IKHYDRPEML 

       310        320        330        340        350        360 
GLYNGLEAAM EEAKQIKPNL DYPAGPTYNL MGFDTEMFTP LFIAARITGW TAHIMEQVAD 

       370 
NALIRPLSEY NGPEQRQVP 

« Hide

References

[1]"Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R."
Gerike U., Danson M.J., Russell N.J., Hough D.W.
Eur. J. Biochem. 248:49-57(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium."
Russell R.J., Gerike U., Danson M.J., Hough D.W., Taylor G.L.
Structure 6:351-361(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85944 Genomic DNA. Translation: AAC45662.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A59X-ray2.09A2-379[»]
ProteinModelPortalO34002.
SMRO34002. Positions 3-379.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00223; UER00717.

Family and domain databases

Gene3D1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProIPR011278. 2-MeCitrate/Citrate_synth_I.
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]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFPIRSF001369. Citrate_synth. 1 hit.
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
TIGRFAMsTIGR01800. cit_synth_II. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO34002.

Entry information

Entry nameCISY_ABDS2
AccessionPrimary (citable) accession number: O34002
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: October 16, 2013
This is version 70 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways