ID A0A151P621_ALLMI Unreviewed; 412 AA.
AC A0A151P621;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN Name=GOT1 {ECO:0000313|EMBL:KYO44521.1};
GN ORFNames=Y1Q_0011910 {ECO:0000313|EMBL:KYO44521.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO44521.1};
RN [1] {ECO:0000313|EMBL:KYO44521.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO44521.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-aminobutanoate + 2-oxoglutarate = 2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:70223, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000256|ARBA:ARBA00036027};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70225;
CC Evidence={ECO:0000256|ARBA:ARBA00036027};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-sulfino-L-alanine = 3-sulfinopyruvate + L-
CC glutamate; Xref=Rhea:RHEA:70295, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:61085, ChEBI:CHEBI:140699;
CC Evidence={ECO:0000256|ARBA:ARBA00036106};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70297;
CC Evidence={ECO:0000256|ARBA:ARBA00036106};
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|ARBA:ARBA00036008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825;
CC Evidence={ECO:0000256|ARBA:ARBA00036008};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-cysteine = 2-oxo-3-sulfanylpropanoate + L-
CC glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678; EC=2.6.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00036988};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442;
CC Evidence={ECO:0000256|ARBA:ARBA00036988};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO44521.1}.
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DR EMBL; AKHW03000742; KYO44521.1; -; Genomic_DNA.
DR RefSeq; XP_014464939.1; XM_014609453.2.
DR AlphaFoldDB; A0A151P621; -.
DR STRING; 8496.A0A151P621; -.
DR GeneID; 102566110; -.
DR KEGG; amj:102566110; -.
DR CTD; 2805; -.
DR eggNOG; KOG1412; Eukaryota.
DR OrthoDB; 1123851at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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:SF3; ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000256|RuleBase:RU000480,
KW ECO:0000313|EMBL:KYO44521.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transferase {ECO:0000256|RuleBase:RU000480, ECO:0000313|EMBL:KYO44521.1}.
FT DOMAIN 31..404
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 412 AA; 45841 MW; 2815D887C31D0DAD CRC64;
MAASVFAAVP QAAPVAVFQL TADFRQDPAA RKVNLGVGAY RTDEGQPWVL PVVRKVEQMI
ASDTSLNHEY LPILGLPDFR ANASRIALGD DSPAIEEGRV GGVQSLGGTG ALRIGAEFLR
RWYNGNNNTA TPVYISSPSW ENHNSVFTDA GFKDIRTYRY WDPAKRGLDL QGLLEDMEAA
PEFSIFILHA CAHNPTGTDP TQEQWKQIAT VMKRRFLFPF FDSAYQGFAS GCLDRDAWAV
RYFVAQGFEL FCAQSFSKNF GLYNERVGNL SVVGKDANNV QRVLSQMEKI ARTTWSNPPS
QGARIVATTL TSPQLFAEWK DNVKTMADRV LLMRSELRSR LESLGTPGTW SHITDQIGMF
SFTGLNPKQV DYMIKEKHIY LMASGRINMC GLTTKNLDYV ASSIHEAVTK IQ
//
