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P34085

- CISY_NEUCR

UniProt

P34085 - CISY_NEUCR

Protein

Citrate synthase, mitochondrial

Gene

cit-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (30 Apr 2003)
      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 sitei352 – 3521PROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetyl-CoA catabolic process Source: EnsemblFungi
    2. cellular carbohydrate metabolic process Source: InterPro
    3. 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, mitochondrial (EC:2.3.3.16)
    Gene namesi
    Name:cit-1
    ORF Names:B1D1.330, NCU01692
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 6, Linkage Group II

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. peroxisome Source: EnsemblFungi

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
    BLAST
    Chaini34 – 469436Citrate synthase, mitochondrialPRO_0000005480Add
    BLAST

    Proteomic databases

    PRIDEiP34085.

    Expressioni

    Developmental stagei

    Abundant after 6-12 hours of growth. It is not significantly expressed after 24 hours, which is several hours after entering the stationary phase of growth.

    Interactioni

    Protein-protein interaction databases

    STRINGi5141.NCU01692.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP34085.
    SMRiP34085. Positions 33-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000130831.
    KOiK01647.
    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.

    P34085-1 [UniParc]FASTAAdd to Basket

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    MAPVMRLGSA ALRSSIHLTS RQTAFTAARC YSSKTQTLKE RFAELLPENI    50
    EKIKALRKEH GSKVVDKVTL DQVYGGARGI KCLVWEGSVL DAEEGIRFRG 100
    KTIPECQELL PKAPGGKEPL PEGLFWLLLT GEVPSEQQVR DLSAEWAARS 150
    DVPKFIEELI DRCPSDLHPM AQLSLAVTAL EHTSSFARAY AKGINKKEYW 200
    GYTFEDSMDL IAKLPTIAAR IYQNVFKGGK VAAVQKDKDY SFNFANQLGF 250
    GDNKDFVELL RLYLTIHTDH EGGNVSAHTT HLVGSALSSP FLSVAAGLNG 300
    LAGPLHGLAN QEVLNWLTEM KKVIGDDLSD EAITKYLWDT LNAGRVVPGY 350
    GHAVLRKTDP RYSAQRKFAQ EHLPEDPMFQ LVSQVYKIAP KVLTEHGKTK 400
    NPYPNVDAHS GVLLQHYGLT EANYYTVLFG VSRAIGVLPQ LIIDRAVGAP 450
    IERPKSYSTD KWIEICKKL 469
    Length:469
    Mass (Da):51,989
    Last modified:April 30, 2003 - v2
    Checksum:iC14FFDDE07D345FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti351 – 3511G → A in AAA16630. (PubMed:7904043)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84187 Unassigned DNA. Translation: AAA16630.1.
    AL355927 Genomic DNA. Translation: CAB91282.1.
    CM002237 Genomic DNA. Translation: EAA27662.1.
    PIRiS41563.
    RefSeqiXP_956898.1. XM_951805.2.
    UniGeneiNcr.20011.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000001887; EFNCRP00000001887; EFNCRG00000001885.
    GeneIDi3873020.
    KEGGincr:NCU01692.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84187 Unassigned DNA. Translation: AAA16630.1 .
    AL355927 Genomic DNA. Translation: CAB91282.1 .
    CM002237 Genomic DNA. Translation: EAA27662.1 .
    PIRi S41563.
    RefSeqi XP_956898.1. XM_951805.2.
    UniGenei Ncr.20011.

    3D structure databases

    ProteinModelPortali P34085.
    SMRi P34085. Positions 33-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU01692.1.

    Proteomic databases

    PRIDEi P34085.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000001887 ; EFNCRP00000001887 ; EFNCRG00000001885 .
    GeneIDi 3873020.
    KEGGi ncr:NCU01692.

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000130831.
    KOi K01647.
    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. "Characterization of the cit-1 gene from Neurospora crassa encoding the mitochondrial form of citrate synthase."
      Ferea T., Contreras E.T., Oung T., Bowman E.J., Bowman B.J.
      Mol. Gen. Genet. 242:105-110(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: 74A.
    2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
      Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
      Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    3. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

    Entry informationi

    Entry nameiCISY_NEUCR
    AccessioniPrimary (citable) accession number: P34085
    Secondary accession number(s): Q7RY26, Q9P688
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 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