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P26563

- AATM_LUPAN

UniProt

P26563 - AATM_LUPAN

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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

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 nitrogen By similarity
Binding sitei182 – 1821Aspartate By similarity
Binding sitei235 – 2351Aspartate By similarity
Binding sitei428 – 4281Aspartate By 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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei‹1 – 49›49Mitochondrion Reviewed prediction
Add
BLAST
Chaini50 – 454405Aspartate aminotransferase P2, mitochondrial
PRO_0000001212Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiP26563.
ProMEXiP26563.

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP26563.
SMRiP26563. Positions 52-448.

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

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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

Non-terminal residue

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...

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: February 19, 2014
This is version 86 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

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