P05202 (AATM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate aminotransferase, mitochondrial
Short name=mAspAT
EC=2.6.1.1
EC=2.6.1.7

Alternative name(s):
Fatty acid-binding protein
Short name=FABP-1
Glutamate oxaloacetate transaminase 2
Kynurenine aminotransferase 4
Kynurenine aminotransferase IV
Kynurenine--oxoglutarate transaminase 4
Kynurenine--oxoglutarate transaminase IV
Plasma membrane-associated fatty acid-binding protein
Short name=FABPpm
Transaminase A

Gene names

Name:	Got2
Synonyms:	Got-2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	430 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	Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids. Ref.7 Ref.12
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Ref.10 Ref.12 L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. Ref.10 Ref.12
Cofactor	Pyridoxal phosphate. Ref.12
Subunit structure	Homodimer. Ref.11 Ref.12
Subcellular location	Mitochondrion matrix. Cell membrane Ref.3 Ref.7.
Tissue specificity	Detected in brain (at protein level). Ref.10
Post-translational modification	Acetylation of Lys-296, Lys-345 and Lys-363 is observed in liver mitochondria from fasted mice but not from fed mice.
Miscellaneous	In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cell membrane Membrane Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation Nitration
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aspartate biosynthetic process Inferred from direct assay PubMed 4193185. Source: MGI aspartate catabolic process Inferred from electronic annotation. Source: Compara fatty acid transport Inferred from electronic annotation. Source: Compara glutamate catabolic process to 2-oxoglutarate Inferred from direct assay PubMed 4193185. Source: MGI glutamate catabolic process to aspartate Inferred from direct assay PubMed 4193185. Source: MGI oxaloacetate metabolic process Inferred from direct assay PubMed 4193185. Source: MGI response to ethanol Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC kynurenine-oxoglutarate transaminase 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

Transit peptide

1 – 29

29

Mitochondrion

Chain

30 – 430

401

Aspartate aminotransferase, mitochondrial

PRO_0000001216

Sites

Binding site

65

1

Substrate; via amide nitrogen By similarity

Binding site

162

1

Substrate By similarity

Binding site

215

1

Substrate

Binding site

407

1

Substrate

Amino acid modifications

Modified residue

73

1

N6-acetyllysine By similarity

Modified residue

90

1

N6-acetyllysine By similarity

Modified residue

94

1

N6-acetyllysine Ref.9

Modified residue

96

1

Nitrated tyrosine Ref.8

Modified residue

159

1

N6-acetyllysine Ref.9

Modified residue

185

1

N6-acetyllysine Ref.9

Modified residue

234

1

N6-acetyllysine By similarity

Modified residue

279

1

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

296

1

N6-acetyllysine Ref.9

Modified residue

309

1

N6-succinyllysine By similarity

Modified residue

345

1

N6-acetyllysine Ref.9

Modified residue

363

1

N6-acetyllysine Ref.9

Modified residue

396

1

N6-acetyllysine By similarity

Modified residue

404

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

68

1

R → G in BAE39800. Ref.4

Sequence conflict

146

1

Q → E in AAB91426. Ref.3

Sequence conflict

153

1

R → G in BAE39800. Ref.4

Sequence conflict

377

1

Q → K in BAE39800. Ref.4

Sequence conflict

421

1

L → I in BAE39800. Ref.4

Secondary structure

1

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430

Helix Strand Turn

Details...

Turn

32 – 35

4

Helix

43 – 53

11

Helix

78 – 89

12

Helix

103 – 114

12

Helix

119 – 123

5

Beta strand

126 – 132

7

Helix

133 – 148

16

Beta strand

153 – 160

8

Helix

165 – 172

8

Beta strand

175 – 180

6

Turn

184 – 186

3

Beta strand

187 – 189

3

Helix

191 – 199

9

Beta strand

206 – 211

6

Turn

215 – 217

3

Helix

223 – 235

13

Beta strand

239 – 245

7

Turn

247 – 251

5

Helix

254 – 257

4

Helix

259 – 266

8

Beta strand

272 – 276

5

Turn

278 – 280

3

Helix

284 – 286

3

Beta strand

288 – 294

7

Helix

298 – 316

19

Helix

322 – 332

11

Helix

334 – 365

32

Helix

373 – 376

4

Beta strand

379 – 383

5

Helix

388 – 397

10

Beta strand

406 – 409

4

Helix

410 – 412

3

Turn

415 – 417

3

Helix

418 – 429

12

Sequences

	Sequence		Length	Mass (Da)
	P05202 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: D590524CA7FFB885	FASTA	430	47,411
	10 20 30 40 50 60 MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM 70 80 90 100 110 120 NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENNEV 130 140 150 160 170 180 LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR 190 200 210 220 230 240 YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA 250 260 270 280 290 300 FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE 310 320 330 340 350 360 AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS 370 380 390 400 410 420 NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY 430 LAHAIHQVTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase isoenzymes." Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y. J. Biol. Chem. 261:16976-16983(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural organization of the mouse mitochondrial aspartate aminotransferase gene." Tsuzuki T., Obaru K., Setoyama C., Shimada K. J. Mol. Biol. 198:21-31(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H/He. Tissue: Liver.
[3]	"Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA." Bradbury M.W., Berk P.D. Biochem. J. 345:423-427(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Strain: FVB. Tissue: Liver.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c, C57BL/6J and NOD. Tissue: Bone marrow macrophage, Cecum, Dendritic cell and Melanocyte.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain and Eye.
[6]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 60-81; 91-122; 126-139; 171-180; 186-200; 280-296; 310-345; 356-363 AND 397-404, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[7]	"Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake." Zhou S.-L., Stump D., Kiang C.L., Isola L.M., Berk P.D. Proc. Soc. Exp. Biol. Med. 208:263-270(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-159; LYS-185; LYS-296; LYS-345 AND LYS-363, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain." Guidetti P., Amori L., Sapko M.T., Okuno E., Schwarcz R. J. Neurochem. 102:103-111(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[11]	"Structure, expression, and function of kynurenine aminotransferases in human and rodent brains." Han Q., Cai T., Tagle D.A., Li J. Cell. Mol. Life Sci. 67:353-368(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 30-430 IN COMPLEX WITH SYNTHETIC INHIBITOR, SUBUNIT.
[12]	"Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV." Han Q., Robinson H., Cai T., Tagle D.A., Li J. Biosci. Rep. 31:323-332(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 30-430 IN COMPLEX WITH L-KYNURENINE; OXALOACETATE AND PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02622 mRNA. Translation: AAA37264.1.
X06917 , X06918, X06919, X06920, X06921, X06922, X06923, X06924, X06925, X06926 Genomic DNA. Translation: CAA30015.1.
M37259 , M37250, M37251, M37252, M37253, M37254, M37255, M37256, M37258 Genomic DNA. Translation: AAA37265.1. Sequence problems.
U82470 mRNA. Translation: AAB91426.1.
AK136556 mRNA. Translation: BAE23042.1.
AK147953 mRNA. Translation: BAE28248.1.
AK149886 mRNA. Translation: BAE29146.1.
AK149926 mRNA. Translation: BAE29171.1.
AK150194 mRNA. Translation: BAE29370.1.
AK152921 mRNA. Translation: BAE31596.1.
AK155075 mRNA. Translation: BAE33029.1.
AK167767 mRNA. Translation: BAE39800.1.
BC089015 mRNA. Translation: AAH89015.1.
BC089341 mRNA. Translation: AAH89341.1.

IPI

IPI00117312.

PIR

S01174.

RefSeq

NP_034455.1. NM_010325.2.

UniGene

Mm.230169.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HLM	X-ray	2.50	A/B/C/D	30-430	[»]
3PD6	X-ray	2.40	A/B/C/D	30-430	[»]
3PDB	X-ray	2.40	A/B/C/D	30-430	[»]

ProteinModelPortal

P05202.

SMR

P05202. Positions 30-430.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05202. 1 interaction.

PTM databases

PhosphoSite

P05202.

Proteomic databases

PaxDb

P05202.

PRIDE

P05202.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672.

GeneID

14719.

KEGG

mmu:14719.

UCSC

uc009mzi.1. mouse.

Organism-specific databases

CTD

2806.

MGI

MGI:95792. Got2.

Phylogenomic databases

eggNOG

COG1448.

GeneTree

ENSGT00390000014081.

HOGENOM

HOG000185898.

HOVERGEN

HBG000951.

InParanoid

P05202.

KO

K14455.

OMA

DFTGAIE.

OrthoDB

EOG4RXZ07.

Gene expression databases

Bgee

P05202.

Genevestigator

P05202.

GermOnline

ENSMUSG00000031672. Mus musculus.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.

InterPro

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

PANTHER

PTHR11879. PTHR11879. 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...

Other

ChEMBL

CHEMBL3647.

EvolutionaryTrace

P05202.

NextBio

286731.

SOURCE

Search...

Entry information

Entry name

AATM_MOUSE

Accession

Primary (citable) accession number: P05202
Secondary accession number(s): O09188 , Q3TIP6, Q3UD91, Q5HZH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program