ID A0A059LSC6_9CHLO Unreviewed; 547 AA.
AC A0A059LSC6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=H632_c57p3 {ECO:0000313|EMBL:KDD76954.1};
OS Helicosporidium sp. ATCC 50920.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium.
OX NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD76954.1, ECO:0000313|Proteomes:UP000026042};
RN [1] {ECO:0000313|EMBL:KDD76954.1, ECO:0000313|Proteomes:UP000026042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD76954.1,
RC ECO:0000313|Proteomes:UP000026042};
RX PubMed=24809511;
RA Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT "A lack of parasitic reduction in the obligate parasitic green alga
RT helicosporidium.";
RL PLoS Genet. 10:E1004355-E1004355(2014).
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:KDD76954.1}.
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DR EMBL; AYPS01000057; KDD76954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059LSC6; -.
DR STRING; 1291522.A0A059LSC6; -.
DR OrthoDB; 313745at2759; -.
DR Proteomes; UP000026042; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR006124; Metalloenzyme.
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; PF01676; Metalloenzyme; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000026042}.
FT DOMAIN 77..166
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 287..486
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 58086 MW; 4047130D87CEC460 CRC64;
MERLEADGAT GDYRSDLSAK MRAAAQAVQG GGGGEEVGGG EVGEERGGGE GGGGEGGGGE
GTGGEGGEKG KAPQPSAIRS SPLDFVMVHI KAVDDAGHDR LTLGKVRLLE AVDKAVGQLV
CRLEGGRGPT GRSREFFVAV TSDHSTPVEG GDHSFEPVPF ALAAVEDVVA ELGGAAALAR
TAPLDEIKLS VTMDDRRTSP RGMASETPYV SAFDESHVVS GYVGNKAAVF PLQLLGFEVD
AVHTVHLSNH TGYPIYKGTV LKSAELWEIV HTMDSNGLLA QITHLLTGFV GSGELMAVFE
RVIRLLRARN PDLVYVCDPV QGDHGILYVS PELPPLFRQL IAHATVLTPN QFEAGLLLNR
PLKGLRDARQ ACEELLDKGP AVVVLTSLDL PAWPQHVTIV AAQRLDGQEG ATVFRELEED
GDALQPCSPR CSFLILRVPR LKAYFTGTGD LLSALLLAHL HREKNSLRPA LEVAVAALQT
VLADTAAHSQ SAADIKSRDA ATCRRQELRL VQNAQALLRP PVQHRARELT EKDLEEDDRA
AAAGENG
//
