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)

P26563

- AATM_LUPAN

UniProt

P26563 - AATM_LUPAN

Protein

Aspartate aminotransferase P2, mitochondrial

Gene
N/A
Organism
Lupinus angustifolius (Narrow-leaved blue lupin)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism.

    Catalytic activityi

    L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.

    Cofactori

    Pyridoxal phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei86 – 861Aspartate; via amide nitrogenBy similarity
    Binding sitei182 – 1821AspartateBy similarity
    Binding sitei235 – 2351AspartateBy similarity
    Binding sitei428 – 4281AspartateBy similarity

    GO - Molecular functioni

    1. L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB
    2. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
    3. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. aspartate metabolic process Source: UniProtKB
    3. biosynthetic process Source: InterPro
    4. glutamate metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate aminotransferase P2, mitochondrial (EC:2.6.1.1)
    Alternative name(s):
    Transaminase A
    OrganismiLupinus angustifolius (Narrow-leaved blue lupin)
    Taxonomic identifieri3871 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeGenisteaeLupinus

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei‹1 – 49›49MitochondrionSequence AnalysisAdd
    BLAST
    Chaini50 – 454405Aspartate aminotransferase P2, mitochondrialPRO_0000001212Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei299 – 2991N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PRIDEiP26563.
    ProMEXiP26563.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP26563.
    SMRiP26563. Positions 52-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view]
    PANTHERiPTHR11879. PTHR11879. 1 hit.
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    PRINTSiPR00799. TRANSAMINASE.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

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

    P26563-1 [UniParc]FASTAAdd to Basket

    « Hide

    SSLLSIPSLS LQYNDKLKVG GNSLRFSKEQ SNTFSNAKSS CRISMVAAVN    50
    VSRFEGIPMA PPDPILGVSE AFRADTSDAK LNLGVGAYRT EELQPYVLKV 100
    VNKAENLMLE RGQNKEYLAI EGLAAFNKAT AELLLGADNP AIKQQRVATV 150
    QGLSGTGSLR LGAALIERYF PGAKVLISAP TWGNHKNIFN DARVPWSEYR 200
    YYDPKTVGLD FEGMIEDIKA APEGTFVLLH GCAHNPTGID PTPEQWEKIA 250
    DVIQEKNHIP FFDVAYQGFA SGSLDEDAAS VRLFVARGLE VLVAQSYSKN 300
    LGLYAERIGA INVISSSPES AARVKSQLKR IARPMYSNPP VHGARIVADI 350
    VGNPALFDEW KVEMEMMAGR IKNVRQQLYD SISSKDKSGK DWSFILKQIG 400
    MFSYTGLNKN QSDNMTNKWH VYMTKDGRIS LAGLSLAKCE YLADAIIDSF 450
    HYVS 454
    Length:454
    Mass (Da):49,916
    Last modified:August 1, 1992 - v1
    Checksum:i744CC12F1D81E739
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59761 mRNA. Translation: CAA42430.1.
    PIRiS22465. XNYLB.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59761 mRNA. Translation: CAA42430.1 .
    PIRi S22465. XNYLB.

    3D structure databases

    ProteinModelPortali P26563.
    SMRi P26563. Positions 52-448.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P26563.
    ProMEXi P26563.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view ]
    PANTHERi PTHR11879. PTHR11879. 1 hit.
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00799. TRANSAMINASE.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a cDNA encoding aspartate aminotransferase-P2 from lupin root nodules."
      Reynolds P.H.S., Smith L.A., Jones W.T., Dickson J.M.J., Jones S.J., Rodber K., Liddane C.P.
      Plant Mol. Biol. 19:465-472(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Uniharvest.
      Tissue: Root nodule.

    Entry informationi

    Entry nameiAATM_LUPAN
    AccessioniPrimary (citable) accession number: P26563
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3