ID A0A200QDB4_9MAGN Unreviewed; 448 AA.
AC A0A200QDB4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:OVA08474.1};
GN ORFNames=BVC80_209g211 {ECO:0000313|EMBL:OVA08474.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA08474.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA08474.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA08474.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
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:OVA08474.1}.
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DR EMBL; MVGT01002328; OVA08474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QDB4; -.
DR STRING; 56857.A0A200QDB4; -.
DR InParanoid; A0A200QDB4; -.
DR OrthoDB; 1328656at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; 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; PTHR43795:SF39; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE 7; 1.
DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OVA08474.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Transferase {ECO:0000313|EMBL:OVA08474.1}.
FT DOMAIN 54..435
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 448 AA; 50516 MW; 48952B62DAF7CC5E CRC64;
MAIEIEQPTA AASTVELSRV AVSDTHGEDS PYFAGWKAYD ENPYDESSNP SGVIQMGLAE
NQVSFDLLEE YLEQHSAQPT PKKISGFSSF RENALFQDYH GLQSFRMAMA SFMEKIRGDK
AKFDPERVVL TAGATAANEL LTFILANPGD ALLVPTPYYP GFDRDLRWRT GVKIVPVHCN
SANNFQVTLQ ALEDAYKKAE SMNIKVRGLL ITNPSNPLGI AIERSVLEEI LDFVTRKNIH
LVSDEIYSGS VFSSTEFVSI AEIIEARNYE DAERVHIVYS LSKDLGLPGF RVGTIYSYND
RVVTTARRMS SFSLVSSQTQ HLLASMLSDT EFTENYIKIN RERLNKRYEF IIDGLRKAGI
ECLQGNAGLF CWMNLSPFLE NPTRESELVL WNSILKEVKL NISPGSSCHC DEPGWFRVCF
ANMSLQTLQV ALKRIHDFIE VQRKLKRN
//
