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P20903

- CISY_STRHY

UniProt

P20903 - CISY_STRHY

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Protein

Citrate synthase

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

Functioni

Catalytic activityi

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

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.

Sequencei

Sequence statusi: Fragment.

P20903-1 [UniParc]FASTAAdd to Basket

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

Non-terminal residue

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

Sequence databases

PIRiPQ0046.

Cross-referencesi

Sequence databases

PIRi PQ0046.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .

Family and domain databases

ProtoNeti Search...

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: June 11, 2014
This is version 52 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

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