ID A0A2V0P7U1_9CHLO Unreviewed; 377 AA.
AC A0A2V0P7U1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=Rsub_06192 {ECO:0000313|EMBL:GBF93943.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF93943.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF93943.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF93943.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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:GBF93943.1}.
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; BDRX01000046; GBF93943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0P7U1; -.
DR STRING; 307507.A0A2V0P7U1; -.
DR InParanoid; A0A2V0P7U1; -.
DR Proteomes; UP000247498; 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:GBF93943.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW Transferase {ECO:0000313|EMBL:GBF93943.1}.
FT DOMAIN 93..199
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 38653 MW; B8345AA6BE4DD5C7 CRC64;
MAAAPGERGA VAGAAGAPGR EGGRVLSIQS HVVSGYVGNK SATLPLQLLG FDVDPVMSVQ
FSNHTGYPTI KGKAFGGDHL LELLEARAHG GYIGTLSLLE AIATVARTLR AANPQLTYVC
DPVLGDDGHC YVEKDLIGAY KTTILPLASI LTPNSFEAGL LTGLPVRDEA EALAACDALH
ALGPHTVVIT SMDLAGDASS SQPASGGQPA SSSQPASDGG DKDGDPAADG PLRPVPGAYI
SLVASTRQEQ LPGRPSAFRI RIPKLDAYFT GTGDLLSALL LAWCARHPAD LALAVEKAVA
GLQAVLRVTA AAVHETERRE GSAGGGGGGG GGAHDLLSSK GRTAAVFRAK ELRLVQARHA
LVDPEVELRA EPLRRGQ
//
