ID   C3ZMD6_BRAFL            Unreviewed;       439 AA.
AC   C3ZMD6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Aminotransferase class III-fold pyridoxal phosphate-dependent enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BRAFLDRAFT_76656 {ECO:0000313|EMBL:EEN46392.1};
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:EEN46392.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN46392.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN46392.1};
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   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; GG666644; EEN46392.1; -; Genomic_DNA.
DR   RefSeq; XP_002590381.1; XM_002590335.1.
DR   AlphaFoldDB; C3ZMD6; -.
DR   STRING; 7739.C3ZMD6; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   InParanoid; C3ZMD6; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
SQ   SEQUENCE   439 AA;  48376 MW;  7B80E18CEFED50BC CRC64;
     MDPETNGSTL GQAAQRSLDV FPAGSNGEFN LPKDLTTVLS RGKDCYVWDV DGKWYLDFSM
     GWGTNLVGHA REEVVAAVTE QAAHGSNFAY VNEKSLQLAE EIKRMSPAVE YLSAGIEHSV
     KHHVLVAPYN DLSMTTEIVE QHRGDLAAVI VEPLHRCTPP MDGFLQGLRD LTKKHDVLLI
     FDEVVTGFRL AYGGAQEYYG VIPDLVGYGK ALGGGYPIGV FGGRADIMSL VNEDLLGKDE
     RYVWTASSLG CNTISASAAL AALQIYRRTG TYQQLHHIGR YVRNKMKECL EKNDISGHVI
     GDGPLAQVLF TEKLVYNYRE QKLQENTARR RAMMVGLFKR GVFLNPMGTK LYLSLKHTEE
     IHHPLIIKTG GNHSGNHPLI IKTGGNHSGN HPLIIKTGGN HSGNHPLIIK AGGNYRTLRR
     GTHLANMPYI PLSFTCNTM
//