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Protein

Citrate synthase

Gene

gltA

Organism
Streptomyces hygroscopicus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

Enzyme regulationi

Allosterically inhibited by NADH.

Pathwayi

GO - Molecular functioni

  1. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
OrganismiStreptomyces hygroscopicus
Taxonomic identifieri1912 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›20›20Citrate synthasePRO_0000169972Add
BLAST

Interactioni

Subunit structurei

Homohexamer.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Sequencei

Sequence statusi: Fragment.

P20903-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20
SDNSVVLRYG DGEYSYPVVD
Length:20
Mass (Da):2,234
Last modified:February 1, 1991 - v1
Checksum:iC527EC7A87119597
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei20 – 201

Sequence databases

PIRiPQ0046.

Cross-referencesi

Sequence databases

PIRiPQ0046.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCISY_STRHY
AccessioniPrimary (citable) accession number: P20903
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 1, 2014
This is version 53 of the entry and version 1 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

Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.