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O34002

- CISY_ABDS2

UniProt

O34002 - CISY_ABDS2

Protein

Citrate synthase

Gene

gltA

Organism
Antarctic bacterium DS2-3R
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Temperature dependencei

    Optimum temperature is 31 degrees Celsius. Cold-active. Is rapidly inactivated at 45 degrees Celsius, and shows significant activity at 10 degrees Celsius and below.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei270 – 2701PROSITE-ProRule annotation
    Active sitei321 – 3211PROSITE-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
    Synonyms:cisY
    OrganismiAntarctic bacterium DS2-3R
    Taxonomic identifieri56673 [NCBI]
    Taxonomic lineageiBacteria

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 379379Citrate synthasePRO_0000169925Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    379
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 103
    Beta strandi19 – 246
    Turni25 – 284
    Beta strandi29 – 324
    Helixi37 – 437
    Helixi46 – 5510
    Helixi61 – 7212
    Helixi79 – 857
    Helixi94 – 10714
    Turni110 – 1134
    Helixi117 – 14226
    Helixi156 – 16510
    Helixi171 – 18414
    Helixi191 – 20010
    Turni201 – 2033
    Helixi206 – 21813
    Turni220 – 2245
    Helixi225 – 23511
    Helixi244 – 26017
    Helixi280 – 29314
    Helixi298 – 31417
    Helixi321 – 33010
    Helixi335 – 3373
    Helixi338 – 35922

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A59X-ray2.09A2-379[»]
    ProteinModelPortaliO34002.
    SMRiO34002. Positions 3-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO34002.

    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.

    O34002-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEPTIHKGL AGVTADVTAI SKVNSDTNSL LYRGYPVQEL AAKCSFEQVA    50
    YLLWNSELPN DSELKAFVNF ERSHRKLDEN VKGAIDLLST ACHPMDVART 100
    AVSVLGANHA RAQDSSPEAN LEKAMSLLAT FPSVVAYDQR RRRGEELIEP 150
    REDLDYSANF LWMTFGEEAA PEVVEAFNVS MILYAEHSFN ASTFTARVIT 200
    STLADLHSAV TGAIGALKGP LHGGANEAVM HTFEEIGIRK DESLDEAATR 250
    SKAWMVDALA QKKKVMGFGH RVYKNGDSRV PTMKSALDAM IKHYDRPEML 300
    GLYNGLEAAM EEAKQIKPNL DYPAGPTYNL MGFDTEMFTP LFIAARITGW 350
    TAHIMEQVAD NALIRPLSEY NGPEQRQVP 379
    Length:379
    Mass (Da):41,832
    Last modified:January 1, 1998 - v1
    Checksum:i7D8F4614E3D1CC9F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85944 Genomic DNA. Translation: AAC45662.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85944 Genomic DNA. Translation: AAC45662.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A59 X-ray 2.09 A 2-379 [» ]
    ProteinModelPortali O34002.
    SMRi O34002. Positions 3-379.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .

    Miscellaneous databases

    EvolutionaryTracei O34002.

    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. "Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R."
      Gerike U., Danson M.J., Russell N.J., Hough D.W.
      Eur. J. Biochem. 248:49-57(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium."
      Russell R.J., Gerike U., Danson M.J., Hough D.W., Taylor G.L.
      Structure 6:351-361(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS).

    Entry informationi

    Entry nameiCISY_ABDS2
    AccessioniPrimary (citable) accession number: O34002
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 1, 1998
    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

    3D-structure, Allosteric enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3