ID A0A067JG37_JATCU Unreviewed; 477 AA.
AC A0A067JG37;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDP22797.1};
GN ORFNames=JCGZ_00384 {ECO:0000313|EMBL:KDP22797.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP22797.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP22797.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP22797.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK915374; KDP22797.1; -; Genomic_DNA.
DR RefSeq; XP_012089723.1; XM_012234333.1.
DR AlphaFoldDB; A0A067JG37; -.
DR STRING; 180498.A0A067JG37; -.
DR GeneID; 105648063; -.
DR KEGG; jcu:105648063; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_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; 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; PTHR45688:SF13; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2 HOMOLOG 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138}.
SQ SEQUENCE 477 AA; 52184 MW; D6E44769B97D80D6 CRC64;
MQRFVAKRLL SGRSSLSIHR CFSQLAQNEA SVLDNDALIP KMPPFDYSPP PYTGPSSEEI
MTKRKEFLSP SLFHFYKKPL NVVDGKMQYL FDENGRRYLD AFGGIATVCC GHCHPDIIDS
IVNQIKRLQH STVLYLNHAI ADFAEALASK MPGNLKVVFF TNSGTEANEL AMMIARLYTG
SHDIISLRNA YHGNAAGTMG ATAQSIWKFN VIQSGVHHAL NPDPYRGVFG SDGEKYAKDV
QDIINFGTSG HVAGFISEAI QGVGGIIELA AGYLPAVYKS IKNAGGLCIA DEVQAGFART
GSHFWGFESQ GVVPDIVTMA KGIGNGIPLG AVVTTPEIAE VLTRRSYFNT FGGNPVCTAA
GLAVLKVIEK EKLQENAFVV GTYLKKRLTE LKDKYEIIGD VRGKGLMLGV ELVTDHQHKT
PAKNETLHIM DQMKEMGVLV GKGGFYGNVF RITPPLCFTK EDADFFVDVM DYTMSKM
//