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P26491

- CISY_MYCSM

UniProt

P26491 - CISY_MYCSM

Protein

Citrate synthase

Gene

gltA

Organism
Mycobacterium smegmatis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Enzyme regulationi

    Allosterically inhibited by NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei266 – 2661PROSITE-ProRule annotation
    Active sitei317 – 3171PROSITE-ProRule annotation

    GO - Molecular functioni

    1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer Source: InterPro

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. 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
    OrganismiMycobacterium smegmatis
    Taxonomic identifieri1772 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Citrate synthasePRO_0000169951Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.

    Structurei

    3D structure databases

    ProteinModelPortaliP26491.
    SMRiP26491. Positions 10-374.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Family and domain databases

    Gene3Di1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
    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]
    PANTHERiPTHR11739. PTHR11739. 1 hit.
    PfamiPF00285. Citrate_synt. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001369. Citrate_synth. 1 hit.
    PRINTSiPR00143. CITRTSNTHASE.
    SUPFAMiSSF48256. SSF48256. 1 hit.
    TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
    PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P26491-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTATESEAP RIHKGLAGVV VDTTAISKVV PETNSLTYRG YPVQDLAAQC    50
    SFEQVAYLLW HGELPTDQLA LFSQRERASR RIDRSMQALL AKLPDNCHPM 100
    DVVRTAISYL GAEDLEEDVD TAEANYAKSL RMFAVLPTIV ATDIRRRQGL 150
    TPIPPHSQLG YAQNFLNMCF GEVPEPVVVR AFEQSMVLYA EHSFNASTFA 200
    ARVVTSTQSD IYSAVTAAIG ALKGSLHGGA NEAVMHDMLE IGSAEKAPEW 250
    LHGKLSRKEK VMGFGHRVYK NGDSRVPTMK VALEQVAQVR DGQRWLDIYN 300
    TLESAMFAAT RIKPNLDFPT GPAYYLMDFP IESFTPLFVM SRITGWTAHI 350
    MEQAASNALI RPLSEYSGQP QRSLV 375
    Length:375
    Mass (Da):41,501
    Last modified:August 1, 1992 - v1
    Checksum:i95D6D4E0C954C994
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60513 Genomic DNA. Translation: CAA43028.1.
    PIRiS17168. YKMY.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60513 Genomic DNA. Translation: CAA43028.1 .
    PIRi S17168. YKMY.

    3D structure databases

    ProteinModelPortali P26491.
    SMRi P26491. Positions 10-374.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .

    Family and domain databases

    Gene3Di 1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProi IPR011278. 2-MeCitrate/Citrate_synth_II.
    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 ]
    PANTHERi PTHR11739. PTHR11739. 1 hit.
    Pfami PF00285. Citrate_synt. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001369. Citrate_synth. 1 hit.
    PRINTSi PR00143. CITRTSNTHASE.
    SUPFAMi SSF48256. SSF48256. 1 hit.
    TIGRFAMsi TIGR01800. cit_synth_II. 1 hit.
    PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Citrate synthase from Mycobacterium smegmatis. Cloning, sequence determination and expression in Escherichia coli."
      David M., Lubinsky-Mink S., Benzvi A., Suissa M., Unitzur S., Kuhn J.C.
      Biochem. J. 278:225-234(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692.

    Entry informationi

    Entry nameiCISY_MYCSM
    AccessioniPrimary (citable) accession number: P26491
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 74 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3