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Database: UniProt
Entry: A0A078JQD7_BRANA
LinkDB: A0A078JQD7_BRANA
Original site: A0A078JQD7_BRANA 
ID   A0A078JQD7_BRANA        Unreviewed;       446 AA.
AC   A0A078JQD7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=(rape) hypothetical protein {ECO:0000313|EMBL:CAF2140981.1};
DE   SubName: Full=BnaA02g36300D protein {ECO:0000313|EMBL:CDY68670.1};
GN   Name=BnaA02g36300D {ECO:0000313|EMBL:CDY68670.1};
GN   ORFNames=DARMORV10_A02P23380.1 {ECO:0000313|EMBL:CAF2140981.1},
GN   GSBRNA2T00076587001 {ECO:0000313|EMBL:CDY68670.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY68670.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY68670.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
RN   [2] {ECO:0000313|EMBL:CDY68670.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAF2140981.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope - CEA;
RA   William W.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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; HG994356; CAF2140981.1; -; Genomic_DNA.
DR   EMBL; LK037774; CDY68670.1; -; Genomic_DNA.
DR   STRING; 3708.A0A078JQD7; -.
DR   PaxDb; 3708-A0A078JQD7; -.
DR   EnsemblPlants; CDY68670; CDY68670; GSBRNA2T00076587001.
DR   Gramene; CDY68670; CDY68670; GSBRNA2T00076587001.
DR   OMA; FRIAVNA; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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); 3.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF119; BNAA02G36300D PROTEIN; 1.
DR   Pfam; PF00202; Aminotran_3; 3.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        174..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   446 AA;  48834 MW;  35D6E1AE62353DE4 CRC64;
     MSIFRIAVNA LGHADPDWLQ PVTDQAALLA HVSNVYYTIP QTELSKRLVA SSFAERVFSC
     NSGTEANEAA IKFSRKFQRF THPEDKEVAT SFIAFTNSFH GVTFLEYGNS QAATDLIRSG
     KIADVFVEPI QEEGGVHSAT KEFLQSLRLA CDAAGSLLVF DEVSDNMSRT ILDLFFWFCY
     FSMFSVVWVE VVTYGLWAFE AFGVTPDIMT VAKSLAGGLP IGVMLVTEKV AETIKYGDHG
     SIFAGNPLVC SAAIAVFDKV SKPSFLASVS SKGLYFKDLL VKKLGGNLHV KKVRGEGLII
     GVELDVSASP LVDACCGSRL LILILTAGKG NVVPPLIIEK EEIGRANSAH HEVSNRDSQD
     RYGRWSGDSC IIGKPYDARY GRRYAPYEQR TPYHSKEKYK KGGESGFYKA VNPFAITEGA
     SKALSLQRVQ DDHVVAMASK TDETAR
//
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