ID C3YIV5_BRAFL Unreviewed; 412 AA.
AC C3YIV5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN ORFNames=BRAFLDRAFT_124686 {ECO:0000313|EMBL:EEN59829.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN59829.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59829.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN59829.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; GG666516; EEN59829.1; -; Genomic_DNA.
DR RefSeq; XP_002603818.1; XM_002603772.1.
DR AlphaFoldDB; C3YIV5; -.
DR STRING; 7739.C3YIV5; -.
DR eggNOG; KOG1412; Eukaryota.
DR InParanoid; C3YIV5; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 31..399
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 412 AA; 46039 MW; 5BA465D5F8856DAA CRC64;
MATSRFVDVE LAPPVPVFAL TARYREDNHA NKHNLGVGAY RTDEGLPWVL PVVRTVESQM
AADPILNHEY LPVCGLDSFC KAATKLVLGE DAAAIAQNRA AGVQSLSGTG ALRLGAEFLK
RCLGMNVMYH SKPTWGNHLG IFKDAGFTDI REYRYWDAST KGLDIQGLLE DLRAAPEDSV
VILHACAHNP TGVDPNHSEW EQIMQVVKER RLFPFFDSAY QGFASGDLDR DAYAVRLFEK
SGFEMMIAQS FSKNFGLYNE RTGNLAVVSA DPESLRRVRS QMEKIARPMW SNPPNHGCRI
VATVLGNAAF YAEWKDNIRT MSSRISDMRR LLHEKLRQLK TPGNWDHITN QIGMFSFTGL
GPKQVDYIIN KYHIYLMKNG RINMCAITTS NAEYVASAIN DAVSSVTEDP KL
//
