LOCUS NP_777231 430 aa linear MAM 18-APR-2013
DEFINITION aspartate aminotransferase, mitochondrial [Bos taurus].
ACCESSION NP_777231 XP_614810
VERSION NP_777231.1 GI:27807377
DBSOURCE REFSEQ: accession NM_174806.2
KEYWORDS .
SOURCE Bos taurus (cattle)
ORGANISM Bos taurus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
REFERENCE 1 (residues 1 to 430)
AUTHORS Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
Salzberg,S.L.
TITLE A whole-genome assembly of the domestic cow, Bos taurus
JOURNAL Genome Biol. 10 (4), R42 (2009)
PUBMED 19393038
REFERENCE 2 (residues 1 to 430)
AUTHORS Harhay,G.P., Sonstegard,T.S., Keele,J.W., Heaton,M.P.,
Clawson,M.L., Snelling,W.M., Wiedmann,R.T., Van Tassell,C.P. and
Smith,T.P.
TITLE Characterization of 954 bovine full-CDS cDNA sequences
JOURNAL BMC Genomics 6, 166 (2005)
PUBMED 16305752
REMARK Publication Status: Online-Only
REFERENCE 3 (residues 1 to 430)
AUTHORS Ishiwata,H., Katsuma,S., Kizaki,K., Patel,O.V., Nakano,H.,
Takahashi,T., Imai,K., Hirasawa,A., Shiojima,S., Ikawa,H.,
Suzuki,Y., Tsujimoto,G., Izaike,Y., Todoroki,J. and Hashizume,K.
TITLE Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray
JOURNAL Mol. Reprod. Dev. 65 (1), 9-18 (2003)
PUBMED 12658628
REFERENCE 4 (residues 1 to 430)
AUTHORS Sonstegard,T.S., Capuco,A.V., White,J., Van Tassell,C.P.,
Connor,E.E., Cho,J., Sultana,R., Shade,L., Wray,J.E., Wells,K.D.
and Quackenbush,J.
TITLE Analysis of bovine mammary gland EST and functional annotation of
the Bos taurus gene index
JOURNAL Mamm. Genome 13 (7), 373-379 (2002)
PUBMED 12140684
REFERENCE 5 (residues 1 to 430)
AUTHORS Palmisano,A., Aurilia,V., Ferrara,L., Cubellis,M.V., Sannia,G. and
Marino,G.
TITLE Nucleotide sequence of a cDNA coding for bovine mitochondrial
aspartate aminotransferase
JOURNAL Int. J. Biochem. Cell Biol. 27 (5), 507-511 (1995)
PUBMED 7641080
REFERENCE 6 (residues 1 to 430)
AUTHORS Capasso,S., Garzillo,A.M., Marino,G., Mazzarella,L., Pucci,P. and
Sannia,G.
TITLE Mitochondrial bovine aspartate aminotransferase. Preliminary
sequence and crystallographic data
JOURNAL FEBS Lett. 101 (2), 351-354 (1979)
PUBMED 446759
REFERENCE 7 (residues 1 to 430)
AUTHORS Bossa,F., Polidoro,G., Barra,D., Liverzani,A. and Scandurra,R.
TITLE The phosphopyridoxyl peptide from the mitochondrial aspartate
aminotransferase of beef kidney
JOURNAL Int. J. Pept. Protein Res. 8 (5), 499-501 (1976)
PUBMED 965157
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from Z25466.1.
On Mar 29, 2005 this sequence version replaced gi:61871908.
##Evidence-Data-START##
Transcript exon combination :: Z25466.1, BC102303.1 [ECO:0000332]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..430
/organism="Bos taurus"
/db_xref="taxon:9913"
/chromosome="18"
/map="18"
Protein 1..430
/product="aspartate aminotransferase, mitochondrial"
/EC_number="2.6.1.1"
/note="aspartate aminotransferase 2; FABP-1; FABPpm;
mAspAT; transaminase A; fatty acid-binding protein;
glutamate oxaloacetate transaminase 2; plasma
membrane-associated fatty acid-binding protein; kynurenine
aminotransferase 4; kynurenine aminotransferase IV;
kynurenine--oxoglutarate transaminase 4;
kynurenine--oxoglutarate transaminase IV"
transit_peptide 1..29
/experiment="experimental evidence, no additional details
recorded"
/note="Mitochondrion; propagated from UniProtKB/Swiss-Prot
(P12344.2)"
/calculated_mol_wt=2822
mat_peptide 30..430
/product="Aspartate aminotransferase, mitochondrial"
/experiment="experimental evidence, no additional details
recorded"
/note="propagated from UniProtKB/Swiss-Prot (P12344.2)"
/calculated_mol_wt=44710
Region 35..428
/region_name="PRK09257"
/note="aromatic amino acid aminotransferase; Provisional"
/db_xref="CDD:181731"
Region 60..427
/region_name="AAT_like"
/note="Aspartate aminotransferase family. This family
belongs to pyridoxal phosphate (PLP)-dependent aspartate
aminotransferase superfamily (fold I). Pyridoxal phosphate
combines with an alpha-amino acid to form a compound
called a Schiff base or aldimine...; cd00609"
/db_xref="CDD:99734"
Site order(133..135,162,215,246,276,278..279,287)
/site_type="other"
/note="pyridoxal 5'-phosphate binding site [chemical
binding]"
/db_xref="CDD:99734"
Site order(136,172,239,285..287,323,326)
/site_type="other"
/note="homodimer interface [polypeptide binding]"
/db_xref="CDD:99734"
Site 279
/site_type="active"
/note="catalytic residue [active]"
/db_xref="CDD:99734"
Site 279
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-(pyridoxal phosphate)lysine; propagated from
UniProtKB/Swiss-Prot (P12344.2)"
Site 309
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-succinyllysine; propagated from
UniProtKB/Swiss-Prot (P12344.2)"
CDS 1..430
/gene="GOT2"
/coded_by="NM_174806.2:28..1320"
/db_xref="BGD:BT23188"
/db_xref="GeneID:286886"
ORIGIN
1 mallhsgrfl sgvaaafhpg laaaasaras swwahvemgp pdpilgvtea fkrdtnskkm
61 nlgvgayrdd ngkpyvlpsv rkaeaqiaak nldkeylpia glaefckasa elalgennev
121 lksgryvtvq tisgtgalri gasflqrffk fsrdvflpkp twgnhtpifr dagmqlqsyr
181 yydpktcgfd ftgaiedisk ipaqsvillh acahnptgvd prpeqwkema tvvkknnlfa
241 ffdmayqgfa sgdgnkdawa vrhfieqgin vclcqsyakn mglygervga ftvvckdaee
301 akrvesqlki lirpmysnpp ingariasti ltspdlrkqw lhevkgmadr iismrtqlvs
361 nlkkegsshn wqhiidqigm fcytglkpeq verltkefsi ymtkdgrisv agvtsgnvay
421 lahaihqvtk
//
