ID A0A2I0AF33_9ASPA Unreviewed; 392 AA.
AC A0A2I0AF33;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN Name=PK {ECO:0000313|EMBL:PKA54125.1};
GN ORFNames=AXF42_Ash018135 {ECO:0000313|EMBL:PKA54125.1};
OS Apostasia shenzhenica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Apostasioideae; Apostasia.
OX NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA54125.1, ECO:0000313|Proteomes:UP000236161};
RN [1] {ECO:0000313|EMBL:PKA54125.1, ECO:0000313|Proteomes:UP000236161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC TISSUE=Stem {ECO:0000313|EMBL:PKA54125.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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DR EMBL; KZ451984; PKA54125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0AF33; -.
DR STRING; 1088818.A0A2I0AF33; -.
DR OrthoDB; 5472295at2759; -.
DR Proteomes; UP000236161; Unassembled WGS sequence.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; TIGR00687; pyridox_kin; 1.
DR PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR PANTHER; PTHR10534:SF2; PYRIDOXAL KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:PKA54125.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW Transferase {ECO:0000313|EMBL:PKA54125.1}.
FT DOMAIN 97..195
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 262..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 43474 MW; CD355739679B07E7 CRC64;
MALPPILSLA LPSQTGRVLS IQSHTVQGYV GNKSAVFPLQ LLGYDVDPIN SVQFSNHTGY
PTFRGQVLDG KELWDLIEGL GGNNLLYYTH LLTGYIGSIS FLDTILQVVQ RLRMINPQLI
YVCDPVMGDE GKLYVPKELV SVYREQVVPV ASMLTPNQFE IEQLTGYRIS SEKDGLEACN
KLHAAGPKKV IITSICIQDN FLLIGSHQKE ECAKPLRFNL QGMPPEQFKI VIPKIPAYFT
LLNANQSMAW LFKNNKAYSG SASRQPAGHW QASTTHARQP ARQPALESPE TASVVRARPR
GQLLPAPTPP SRRQTCPPTA APRLASSRLC PRRLSDLRRR RCLRQRGSAA SALPIDTLDC
RRLCSSRSAG HRRRWSPRLC SSDCPTLSPP LC
//
