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Protein

Alanine aminotransferase 2

Gene
N/A
Organism
Panicum miliaceum (Proso millet) (Broomcorn millet)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transfer of C3 units between the cytosol of mesophyll and bundle sheath cells to maintain a nitrogen-carbon balance in the C4-dicarboxylic pathway.

Catalytic activityi

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.

Cofactori

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. biosynthetic process Source: InterPro
  2. L-alanine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17674.
SABIO-RKP34106.
UniPathwayiUPA00322.
UPA00528; UER00586.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine aminotransferase 2 (EC:2.6.1.2)
Short name:
ALAAT-2
Alternative name(s):
Glutamate pyruvate transaminase 2
Short name:
GPT
Glutamic--alanine transaminase 2
Glutamic--pyruvic transaminase 2
OrganismiPanicum miliaceum (Proso millet) (Broomcorn millet)
Taxonomic identifieri4540 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaePaniceaePanicum

Organism-specific databases

GrameneiP34106.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Alanine aminotransferase 2PRO_0000123940Add
BLAST

Amino acid modifications

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

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PRIDEiP34106.

Expressioni

Tissue specificityi

Mesophyll and bundle sheath cells.

Inductioni

By light.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP34106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

P34106-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATVAVENL NPKVLKCEYA VRGEIVIHAQ HLQQQLQTQP GSLPFDEILY
60 70 80 90 100
CNIGNPQSLG QQPVTFFREV LALCDHPCLL EKEETKSLFS ADAISRAKQI
110 120 130 140 150
LSTIPGRATG AYSHSQGIKG LRDAIAAGIA SRDGFPANAD DIFVTDGASP
160 170 180 190 200
GVHMMMQLLI RNEKDGILCP IPQYPLYSAS IALHGGTLVP YYLDEKTGWG
210 220 230 240 250
LEISDLKKQL EDARSKGIDV RALVVINPGN PTGQVLAEDN QCDIVRFCKN
260 270 280 290 300
EGLVLLADEV YQENIYVDDK KFNSFKKIAR SVGYGEDDLP LVSFQSVSKG
310 320 330 340 350
YYGECGKRGG YMEITGFSAP VREQIYKIAS VNLCSNITGQ ILASLVMNPP
360 370 380 390 400
KVGDESYAAY KAEKDGILQS LARRAKALED AFNNLEGISC NKAEGAMYLF
410 420 430 440 450
PQIHLPKKAI EAAKAANKAP DAFYALRLLE STGIVVVPGS GFGQVPGTWH
460 470 480
IRCTILPQED KIPAVITRFK AFHEAFMAEY RD
Length:482
Mass (Da):52,682
Last modified:January 31, 1994 - v1
Checksum:iFB6562233A0D3E21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69421 mRNA. Translation: CAA49199.1.
PIRiS28429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69421 mRNA. Translation: CAA49199.1.
PIRiS28429.

3D structure databases

ProteinModelPortaliP34106.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP34106.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP34106.

Enzyme and pathway databases

UniPathwayiUPA00322.
UPA00528; UER00586.
BioCyciMetaCyc:MONOMER-17674.
SABIO-RKP34106.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of an alanine aminotransferase from NAD-malic enzyme type C4 plant Panicum miliaceum."
    Son D., Sugiyama T.
    Plant Mol. Biol. 20:705-713(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 197-206 AND 308-317.
    Tissue: Leaf.

Entry informationi

Entry nameiALA2_PANMI
AccessioniPrimary (citable) accession number: P34106
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1994
Last sequence update: January 31, 1994
Last modified: November 25, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.