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O00098

- CISY_EMENI

UniProt

O00098 - CISY_EMENI

Protein

Citrate synthase, mitochondrial

Gene

citA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 3 (01 May 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei310 – 3101PROSITE-ProRule annotation
    Active sitei356 – 3561PROSITE-ProRule annotation
    Active sitei411 – 4111PROSITE-ProRule annotation

    GO - Molecular functioni

    1. citrate (Si)-synthase activity Source: ASPGD

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: ASPGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase, mitochondrial (EC:2.3.3.16)
    Gene namesi
    Name:citA
    ORF Names:AN8275
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome II

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: ASPGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535MitochondrionSequence AnalysisAdd
    BLAST
    Chaini36 – 474439Citrate synthase, mitochondrialPRO_0000005477Add
    BLAST

    Proteomic databases

    PRIDEiO00098.

    Structurei

    3D structure databases

    ProteinModelPortaliO00098.
    SMRiO00098. Positions 39-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000130831.
    KOiK01647.
    OMAiELIYEDC.
    OrthoDBiEOG7WQ82G.

    Family and domain databases

    Gene3Di1.10.580.10. 1 hit.
    InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    IPR010109. Citrate_synthase_euk.
    [Graphical view]
    PANTHERiPTHR11739. PTHR11739. 1 hit.
    PfamiPF00285. Citrate_synt. 1 hit.
    [Graphical view]
    PRINTSiPR00143. CITRTSNTHASE.
    SUPFAMiSSF48256. SSF48256. 1 hit.
    TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
    PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O00098-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTLRLSTS ALRSSTLAGK PVVQSVAFNG LRCYSTGKTK SLKETFADKL    50
    PGELEKVKKL RKEHGNKVIG ELTLDQAYGG ARGVKCLVWE GSVLDSEEGI 100
    RFRGLTIPEC QKLLPKAPGG EEPLPEGLFW LLLTGEVPSE QQVRDLSAEW 150
    AARSDLPKFI EELIDRCPST LHPMAQFSLA VTALEHESAF AKAYAKGINK 200
    KEYWHYTFED SMDLIAKLPT IAAKIYRNVF KDGKVAPIQK DKDYSYNLAN 250
    QLGFADNKDF VELMRLYLTI HSDHEGGNVS AHTTHLVGSA LSSPMLSLAA 300
    GLNGLAGPLH GLANQEVLNW LTEMKKVVGN DLSDQSIKDY LWSTLNAGRV 350
    VPGYGHAVLR KTDPRYTSQR EFALRKLPDD PMFKLVSQVY KIAPGVLTEH 400
    GKTKNPYPNV DAHSGVLLQY YGLTEANYYT VLFGVSRALG VLPQLIIDRA 450
    FGAPIERPKS FSTEAYAKLV GAKL 474
    Length:474
    Mass (Da):52,227
    Last modified:May 1, 2007 - v3
    Checksum:i2CA133032DE5C3EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1671C → V in AAC49728. (PubMed:9163747)Curated
    Sequence conflicti167 – 1671C → V in AAM22645. (PubMed:16372000)Curated
    Sequence conflicti194 – 1941Y → T in AAC49728. (PubMed:9163747)Curated
    Sequence conflicti194 – 1941Y → T in AAM22645. (PubMed:16372000)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89675 Genomic DNA. Translation: AAC49728.3.
    AF468824 mRNA. Translation: AAM22645.1.
    AACD01000145 Genomic DNA. Translation: EAA59013.1.
    BN001302 Genomic DNA. Translation: CBF74260.1.
    RefSeqiXP_681544.1. XM_676452.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00004335; CADANIAP00004335; CADANIAG00004335.
    GeneIDi2868998.
    KEGGiani:AN8275.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89675 Genomic DNA. Translation: AAC49728.3 .
    AF468824 mRNA. Translation: AAM22645.1 .
    AACD01000145 Genomic DNA. Translation: EAA59013.1 .
    BN001302 Genomic DNA. Translation: CBF74260.1 .
    RefSeqi XP_681544.1. XM_676452.1.

    3D structure databases

    ProteinModelPortali O00098.
    SMRi O00098. Positions 39-473.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi O00098.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00004335 ; CADANIAP00004335 ; CADANIAG00004335 .
    GeneIDi 2868998.
    KEGGi ani:AN8275.2.

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000130831.
    KOi K01647.
    OMAi ELIYEDC.
    OrthoDBi EOG7WQ82G.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .

    Family and domain databases

    Gene3Di 1.10.580.10. 1 hit.
    InterProi IPR016142. Citrate_synth-like_lrg_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    IPR010109. Citrate_synthase_euk.
    [Graphical view ]
    PANTHERi PTHR11739. PTHR11739. 1 hit.
    Pfami PF00285. Citrate_synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00143. CITRTSNTHASE.
    SUPFAMi SSF48256. SSF48256. 1 hit.
    TIGRFAMsi TIGR01793. cit_synth_euk. 1 hit.
    PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the citA gene encoding the mitochondrial citrate synthase of Aspergillus nidulans."
      Park B.W., Han K.H., Lee C.Y., Lee C.H., Maeng P.J.
      Mol. Cells 7:290-295(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. Seo S.W., Lee C.H., Maeng P.J.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

    Entry informationi

    Entry nameiCISY_EMENI
    AccessioniPrimary (citable) accession number: O00098
    Secondary accession number(s): C8V3P7, Q5ATV5, Q8NKF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Citrate synthase is found in nearly all cells capable of oxidative metabolism.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3