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Protein

Alanine aminotransferase 2

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 3 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: C4 acid pathway

This protein is involved in the pathway C4 acid pathway, which is part of Photosynthesis.
View all proteins of this organism that are known to be involved in the pathway C4 acid pathway and in Photosynthesis.

Pathwayi: L-alanine degradation via transaminase pathway

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from L-alanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Alanine aminotransferase 2
This subpathway is part of the pathway L-alanine degradation via transaminase pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from L-alanine, the pathway L-alanine degradation via transaminase pathway and in Amino-acid degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.2. 2687.
SABIO-RKP52894.
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
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001239391 – 482Alanine aminotransferase 2Add BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei299N6-(pyridoxal phosphate)lysineBy similarity1

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

Secondary structure

1482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Helixi12 – 16Combined sources5
Helixi20 – 22Combined sources3
Helixi24 – 38Combined sources15
Beta strandi42 – 47Combined sources6
Helixi56 – 58Combined sources3
Helixi65 – 75Combined sources11
Helixi77 – 81Combined sources5
Helixi85 – 88Combined sources4
Helixi91 – 101Combined sources11
Beta strandi109 – 111Combined sources3
Helixi119 – 133Combined sources15
Helixi139 – 141Combined sources3
Beta strandi142 – 148Combined sources7
Helixi149 – 159Combined sources11
Beta strandi165 – 172Combined sources8
Helixi176 – 183Combined sources8
Beta strandi187 – 192Combined sources6
Turni195 – 198Combined sources4
Helixi203 – 215Combined sources13
Beta strandi219 – 228Combined sources10
Turni230 – 232Combined sources3
Helixi238 – 251Combined sources14
Beta strandi254 – 258Combined sources5
Turni260 – 263Combined sources4
Helixi275 – 281Combined sources7
Beta strandi285 – 287Combined sources3
Beta strandi291 – 299Combined sources9
Turni300 – 302Combined sources3
Helixi305 – 307Combined sources3
Beta strandi310 – 316Combined sources7
Helixi321 – 330Combined sources10
Helixi337 – 347Combined sources11
Beta strandi352 – 354Combined sources3
Helixi356 – 383Combined sources28
Beta strandi395 – 399Combined sources5
Helixi407 – 416Combined sources10
Helixi420 – 432Combined sources13
Beta strandi437 – 439Combined sources3
Turni440 – 442Combined sources3
Beta strandi450 – 455Combined sources6
Turni459 – 461Combined sources3
Helixi462 – 480Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TCMX-ray2.71A/B1-482[»]
ProteinModelPortaliP52894.
SMRiP52894.
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.

P52894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATVAVDNL NPKVLKCEYA VRGEIVIHAQ RLQEQLKTQP GSLPFDEILY
60 70 80 90 100
CNIGNPQSLG QQPVTFFREV LALCDHPDLL QREEIKTLFS ADSISRAKQI
110 120 130 140 150
LAMIPGRATG AYSHSQGIKG LRDAIASGIA SRDGFPANAD DIFLTDGASP
160 170 180 190 200
GVHLMMQLLI RNEKDGILVP IPQYPLYSAS IALHGGALVP YYLNESTGWG
210 220 230 240 250
LETSDVKKQL EDARSRGINV RALVVINPGN PTGQVLAEEN QYDIVKFCKN
260 270 280 290 300
EGLVLLADEV YQENIYVDNK KFHSFKKIVR SLGYGEEDLP LVSYQSVSKG
310 320 330 340 350
YYGECGKRGG YFEITGFSAP VREQIYKIAS VNLCSNITGQ ILASLVMNPP
360 370 380 390 400
KASDESYASY KAEKDGILAS LARRAKALEH AFNKLEGITC NEAEGAMYVF
410 420 430 440 450
PQICLPQKAI EAAKAANKAP DAFYALRLLE STGIVVVPGS GFGQVPGTWH
460 470 480
FRCTILPQED KIPAVISRFT VFHEAFMSEY RD
Length:482
Mass (Da):52,877
Last modified:October 1, 1996 - v1
Checksum:iE84176F7DFB6B2FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26322 mRNA. Translation: CAA81231.1.
PIRiS42535.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26322 mRNA. Translation: CAA81231.1.
PIRiS42535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TCMX-ray2.71A/B1-482[»]
ProteinModelPortaliP52894.
SMRiP52894.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00322.
UPA00528; UER00586.
BRENDAi2.6.1.2. 2687.
SABIO-RKP52894.

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...

Entry informationi

Entry nameiALA2_HORVU
AccessioniPrimary (citable) accession number: P52894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 76 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

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.