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P20903 (CISY_STRHY) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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=2.3.3.16
Gene names
Name:gltA
OrganismStreptomyces hygroscopicus
Taxonomic identifier1912 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Allosterically inhibited by NADH.

Pathway

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

Subunit structure

Homohexamer.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Molecular functionTransferase
   Technical termAllosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiontransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Citrate synthase
PRO_0000169972

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P20903 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: C527EC7A87119597

FASTA202,234
        10         20 
SDNSVVLRYG DGEYSYPVVD 

« Hide

References

[1]"Purification and characterization of citrate synthase from Streptomyces hygroscopicus SF-1293 and comparison of its properties with those of 2-phosphinomethylmalic acid synthase."
Shimotohno K.W., Imai S., Murakami T., Seto H.
Agric. Biol. Chem. 54:463-470(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 21705 / SF-1293.

Cross-references

Sequence databases

PIRPQ0046.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00223; UER00717.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameCISY_STRHY
AccessionPrimary (citable) accession number: P20903
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 52 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

PATHWAY comments

Index of metabolic and biosynthesis pathways