ID F5HPS6_GLARU Unreviewed; 413 AA.
AC F5HPS6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN Name=GOT-1 {ECO:0000313|EMBL:BAK26556.1};
OS Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Glandirana.
OX NCBI_TaxID=8410 {ECO:0000313|EMBL:BAK26556.1};
RN [1] {ECO:0000313|EMBL:BAK26556.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21328702; DOI=10.1002/jez.668;
RA Suda M., Uno Y., Mori Y., Matsuda Y., Nakamura M.;
RT "Molecular cytogenetic characterization of telomere-specific repetitive DNA
RT sequences in Rana rugosa.";
RL J. Exp. Zool. Part A Ecol. Genet. Physiol. 315:222-231(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000256|RuleBase:RU000480};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU000480}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; AB564277; BAK26556.1; -; mRNA.
DR AlphaFoldDB; F5HPS6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047801; F:L-cysteine transaminase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF55; GLUTAMATE OXALOACETATE TRANSAMINASE 1, ISOFORM B; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase {ECO:0000256|RuleBase:RU000480};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|RuleBase:RU000480}.
FT DOMAIN 32..405
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 413 AA; 46260 MW; DBB045874225A29A CRC64;
MAASSIFSCV PLAPPVAVFK LTADFRADSD PRKVNLGVGA YRTDDSQPWV LPVVKKVEQK
IANDHSLNHE YLPILGLPEF RSSASRIALG EDSPAFKDGR VGGVQSLGGT GALRIGAEFL
RRWYNGTNNT ATPIYISSPS WENHNAVFLD AGFKDIRAYR YWDAAKRGLD LKGLLEDLEN
APEHSIFLLH ACAHNPTGTD PTQEEWKQIA DVMKRRFLFA FFDSAYQGFA SGNLDKDAWA
VRYFVSQGFE LFCAQSFSKN FGLYNERVGN LTVVGKDSDN VSRVLSRMEK IVRTTWSNPP
SQGARIVATT LTTPELFDEW RDNVKTMADR VLLMRAELKS RLEALNTPGT WKHIVEQIGM
FSFTGLNPKQ VEYLIKEKHI YLMASGRINM CGLTTKNLDY VAQSIYEAAT KIH
//
