P52894 (ALA2_HORVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Alanine aminotransferase 2 Short name=ALAAT-2 EC=2.6.1.2 Alternative name(s): Glutamate pyruvate transaminase 2 Short name=GPT Glutamic--alanine transaminase 2 Glutamic--pyruvic transaminase 2
Organism	Hordeum vulgare (Barley)
Taxonomic identifier	4513 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Pathway	Photosynthesis; C4 acid pathway. Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	L-alanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	L-alanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 482

482

Alanine aminotransferase 2

PRO_0000123939

Amino acid modifications

Modified residue

299

1

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

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482

Helix Strand Turn

Details...

Helix

7 – 9

3

Helix

12 – 16

5

Helix

20 – 22

3

Helix

24 – 38

15

Beta strand

42 – 47

6

Helix

56 – 58

3

Helix

65 – 75

11

Helix

77 – 81

5

Helix

85 – 88

4

Helix

91 – 101

11

Beta strand

109 – 111

3

Helix

119 – 133

15

Helix

139 – 141

3

Beta strand

142 – 148

7

Helix

149 – 159

11

Beta strand

165 – 172

8

Helix

176 – 183

8

Beta strand

187 – 192

6

Turn

195 – 198

4

Helix

203 – 215

13

Beta strand

219 – 228

10

Turn

230 – 232

3

Helix

238 – 251

14

Beta strand

254 – 258

5

Turn

260 – 263

4

Helix

275 – 281

7

Beta strand

285 – 287

3

Beta strand

291 – 299

9

Turn

300 – 302

3

Helix

305 – 307

3

Beta strand

310 – 316

7

Helix

321 – 330

10

Helix

337 – 347

11

Beta strand

352 – 354

3

Helix

356 – 383

28

Beta strand

395 – 399

5

Helix

407 – 416

10

Helix

420 – 432

13

Beta strand

437 – 439

3

Turn

440 – 442

3

Beta strand

450 – 455

6

Turn

459 – 461

3

Helix

462 – 480

19

Sequences

	Sequence		Length	Mass (Da)
	P52894 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E84176F7DFB6B2FC	FASTA	482	52,877
	10 20 30 40 50 60 MAATVAVDNL NPKVLKCEYA VRGEIVIHAQ RLQEQLKTQP GSLPFDEILY CNIGNPQSLG 70 80 90 100 110 120 QQPVTFFREV LALCDHPDLL QREEIKTLFS ADSISRAKQI LAMIPGRATG AYSHSQGIKG 130 140 150 160 170 180 LRDAIASGIA SRDGFPANAD DIFLTDGASP GVHLMMQLLI RNEKDGILVP IPQYPLYSAS 190 200 210 220 230 240 IALHGGALVP YYLNESTGWG LETSDVKKQL EDARSRGINV RALVVINPGN PTGQVLAEEN 250 260 270 280 290 300 QYDIVKFCKN EGLVLLADEV YQENIYVDNK KFHSFKKIVR SLGYGEEDLP LVSYQSVSKG 310 320 330 340 350 360 YYGECGKRGG YFEITGFSAP VREQIYKIAS VNLCSNITGQ ILASLVMNPP KASDESYASY 370 380 390 400 410 420 KAEKDGILAS LARRAKALEH AFNKLEGITC NEAEGAMYVF PQICLPQKAI EAAKAANKAP 430 440 450 460 470 480 DAFYALRLLE STGIVVVPGS GFGQVPGTWH FRCTILPQED KIPAVISRFT VFHEAFMSEY RD

References

[1]	"Hypoxically inducible barley alanine aminotransferase: cDNA cloning and expression analysis." Muench D.G., Good A.G. Plant Mol. Biol. 24:417-427(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Himalaya. Tissue: Root.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z26322 mRNA. Translation: CAA81231.1.

PIR

S42535.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TCM	X-ray	2.71	A/B	1-482	[»]

ProteinModelPortal

P52894.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

Gramene

P52894.

Enzyme and pathway databases

UniPathway

UPA00322.
UPA00528; UER00586.

Gene expression databases

Genevestigator

P52894.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ALA2_HORVU

Accession

Primary (citable) accession number: P52894

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program