Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P51044

- CISY_ASPNG

UniProt

P51044 - CISY_ASPNG

Protein

Citrate synthase, mitochondrial

Gene

cit-1

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: 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, mitochondrial (EC:2.3.3.16)
    Gene namesi
    Name:cit-1
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 475Citrate synthase, mitochondrialPRO_0000005475
    Transit peptidei1 – ?MitochondrionBy similarity

    Proteomic databases

    PRIDEiP51044.

    Structurei

    3D structure databases

    ProteinModelPortaliP51044.
    SMRiP51044. Positions 39-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0372.

    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.

    P51044-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTLRLGTS ALRSSSIAAK PVVQSAAFNG LRCYSTGKAK SLKETFAEKL    50
    PAELEKVKKL RKEHGSKVIG EVTLDQAYGG ARGVKCLVWE GSVLDSEEGI 100
    RFRGRTIPEC QELLPKAPGG QEPLPEGLFW LLLTGEIPTE QQVRDLSAEW 150
    AARSDLPKFI EELIDRCPST LHPMSQFSLA VTALEHESAF AKAYAKGINK 200
    KDYWNYTFED SMDLIAKLPT IAAKIYRNVF KDGKVAPIQK DKDYSYNLAN 250
    QLGYGDNNDF VELMRLYLTI HSDHEGGNVS AHTTHLVGSA LSSPMLSLAA 300
    GLNGLAGPLH GLANQEVLNW LTKMKAAIGN DLSDEAIKNY LWSTLNAGQV 350
    VPGYGHAVLR KTDPRYVSQR EFALRKLPDD PMFKLVSQVY KIAPGVLTEH 400
    GKTKNPYPNV DAHSGVLLQY YGLTEANYYT VLFGVSRALG VLPQLIIDRA 450
    LGAPIERPKS YSTELSPSLL VLSCK 475
    Length:475
    Mass (Da):52,154
    Last modified:October 1, 1996 - v1
    Checksum:iF93525B3F31FCB3F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63376 mRNA. Translation: BAA09691.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63376 mRNA. Translation: BAA09691.1 .

    3D structure databases

    ProteinModelPortali P51044.
    SMRi P51044. Positions 39-464.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P51044.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0372.

    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 expression of cDNA encoding Aspergillus niger citrate synthase in Esherichia coli."
      Oshida Y., Miyake K., Kanayama S., Kirimura K., Usami S.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: WU-2223L.

    Entry informationi

    Entry nameiCISY_ASPNG
    AccessioniPrimary (citable) accession number: P51044
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    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 programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Documents

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

    External Data

    Dasty 3