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P20903

- CISY_STRHY

UniProt

P20903 - CISY_STRHY

Protein

Citrate synthase

Gene

gltA

Organism
Streptomyces hygroscopicus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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

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    SDNSVVLRYG DGEYSYPVVD                                    20
    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

    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: 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