P00508 (AATM_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate aminotransferase, mitochondrial
Short name=mAspAT
EC=2.6.1.1

Alternative name(s):
Glutamate oxaloacetate transaminase 2
Transaminase A

Gene names

Name:

GOT2

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids By similarity.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate. Ref.4 Ref.5 Ref.6 Ref.7
Subunit structure	Homodimer. Ref.4 Ref.5 Ref.7
Subcellular location	Mitochondrion matrix Ref.7.
Tissue specificity	Detected in heart (at protein level). Ref.7
Miscellaneous	In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from direct assay Ref.7. Source: UniProtKB L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from physical interaction Ref.7. Source: UniProtKB 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

Transit peptide

1 – 22

22

Mitochondrion Ref.2

Chain

23 – 423

401

Aspartate aminotransferase, mitochondrial

PRO_0000001219

Sites

Binding site

58

1

Aspartate; via amide nitrogen

Binding site

155

1

Aspartate

Binding site

208

1

Aspartate

Binding site

400

1

Aspartate

Amino acid modifications

Modified residue

272

1

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

67

1

S → P AA sequence Ref.2

Sequence conflict

168

1

Q → E AA sequence Ref.2

Sequence conflict

216

1

Q → E AA sequence Ref.2

Secondary structure

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423

Helix Strand Turn

Details...

Turn

25 – 28

4

Helix

36 – 46

11

Helix

71 – 82

12

Helix

96 – 107

12

Helix

112 – 115

4

Beta strand

119 – 125

7

Helix

126 – 141

16

Beta strand

147 – 153

7

Helix

158 – 165

8

Beta strand

168 – 173

6

Turn

177 – 180

4

Helix

184 – 191

8

Beta strand

199 – 206

8

Turn

208 – 210

3

Helix

216 – 228

13

Beta strand

232 – 237

6

Turn

240 – 244

5

Helix

247 – 250

4

Helix

252 – 259

8

Beta strand

265 – 269

5

Turn

271 – 273

3

Helix

277 – 279

3

Beta strand

282 – 287

6

Helix

291 – 309

19

Helix

314 – 325

12

Helix

327 – 357

31

Helix

365 – 369

5

Beta strand

372 – 376

5

Helix

381 – 391

11

Turn

397 – 399

3

Beta strand

400 – 402

3

Helix

403 – 405

3

Turn

408 – 410

3

Helix

411 – 422

12

Sequences

	Sequence		Length	Mass (Da)
	P00508 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: 59D65D4ED4DDF8BA	FASTA	423	47,241
	10 20 30 40 50 60 MALLQSRLLL SAPRRAAATA RASSWWSHVE MGPPDPILGV TEAFKRDTNS KKMNLGVGAY 70 80 90 100 110 120 RDDNGKSYVL NCVRKAEAMI AAKKMDKEYL PIAGLADFTR ASAELALGEN SEAFKSGRYV 130 140 150 160 170 180 TVQGISGTGS LRVGANFLQR FFKFSRDVYL PKPSWGNHTP IFRDAGLQLQ AYRYYDPKTC 190 200 210 220 230 240 SLDFTGAMED ISKIPEKSII LLHACAHNPT GVDPRQEQWK ELASVVKKRN LLAYFDMAYQ 250 260 270 280 290 300 GFASGDINRD AWALRHFIEQ GIDVVLSQSY AKNMGLYGER AGAFTVICRD AEEAKRVESQ 310 320 330 340 350 360 LKILIRPMYS NPPMNGARIA SLILNTPELR KEWLVEVKGM ADRIISMRTQ LVSNLKKEGS 370 380 390 400 410 420 SHNWQHITDQ IGMFCFTGLK PEQVERLTKE FSIYMTKDGR ISVAGVASSN VGYLAHAIHQ VTK

References

[1]	"The primary structure of the precursor of chicken mitochondrial aspartate aminotransferase. Cloning and sequence analysis of cDNA." Jaussi R., Cotton B., Juretic N., Christen P., Schumperli D. J. Biol. Chem. 260:16060-16063(1985) [PubMed: 3840803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The covalent structure of mitochondrial aspartate aminotransferase from chicken. Identification of segments of the polypeptide chain invariant specifically in the mitochondrial isoenzyme." Graf-Hausner U., Wilson K.J., Christen P. J. Biol. Chem. 258:8813-8826(1983) [PubMed: 6345546] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-423.
[3]	"Structure of the genes of two homologous intracellularly heterotopic isoenzymes. Cytosolic and mitochondrial aspartate aminotransferase of chicken." Juretic N., Mattes U., Ziak M., Christen P., Jaussi R. Eur. J. Biochem. 192:119-126(1990) [PubMed: 2401287] [Abstract] Cited for: GENE STRUCTURE. Strain: White leghorn.
[4]	"X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase." McPhalen C.A., Vincent M.G., Jansonius J.N. J. Mol. Biol. 225:495-517(1992) [PubMed: 1593633] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE, PYRIDOXAL PHOSPHATE AT LYS-272, COFACTOR, SUBUNIT.
[5]	"Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase." Malashkevich V.N., Toney M.D., Jansonius J.N. Biochemistry 32:13451-13462(1993) [PubMed: 7903048] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-423 IN COMPLEXES WITH PYRIDOXAL PHOSPHATE; L-ASPARTATE AND L-GLUTAMATE, COFACTOR, SUBUNIT.
[6]	"Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate." von Stosch A.G. Biochemistry 35:15260-15268(1996) [PubMed: 8952476] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-423 IN COMPLEX WITH ERYTHRO-BETA-HYDROXYASPARTATE, COFACTOR.
[7]	"Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase." Markovic-Housley Z., Schirmer T., Hohenester E., Khomutov A.R., Khomutov R.M., Karpeisky M.Y., Sandmeier E., Christen P., Jansonius J.N. Eur. J. Biochem. 236:1025-1032(1996) [PubMed: 8665890] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-423 IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND SUBSTRATE ANALOGS, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M12105 mRNA. Translation: AAA48603.1.

IPI

IPI00598136.

PIR

XNCHDM. A24554.

RefSeq

NP_990854.1. NM_205523.1.

UniGene

Gga.4425.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AKA	X-ray	2.10	A/B	23-423	[»]
1AKB	X-ray	2.30	A	23-423	[»]
1AKC	X-ray	2.30	A	23-423	[»]
1AMA	X-ray	2.30	A	23-423	[»]
1IVR	X-ray	2.40	A	23-423	[»]
1MAP	X-ray	2.40	A	23-423	[»]
1MAQ	X-ray	2.30	A	23-423	[»]
1OXO	X-ray	2.30	A/B	23-423	[»]
1OXP	X-ray	2.50	A	23-423	[»]
1TAR	X-ray	2.20	A/B	23-423	[»]
1TAS	X-ray	2.80	A/B	23-423	[»]
1TAT	X-ray	3.00	A/B	23-423	[»]
7AAT	X-ray	1.90	A/B	23-423	[»]
8AAT	X-ray	2.30	A/B	23-423	[»]
9AAT	X-ray	2.20	A/B	23-423	[»]

ProteinModelPortal

P00508.

SMR

P00508. Positions 23-423.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00508. 1 interaction.

STRING

P00508.

Proteomic databases

PRIDE

P00508.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

396533.

KEGG

gga:396533.

Organism-specific databases

CTD

2806.

Phylogenomic databases

eggNOG

veNOG12918.

GeneTree

ENSGT00390000014081.

HOGENOM

HBG446828.

HOVERGEN

HBG000951.

InParanoid

P00508.

OrthoDB

EOG4RXZ07.

PhylomeDB

P00508.

Family and domain databases

InterPro

IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

KO

K14455.

PANTHER

PTHR11879. Asp_trans. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00799. TRANSAMINASE.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AATM_CHICK

Accession

Primary (citable) accession number: P00508

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1989
Last modified:	January 25, 2012
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program