ID W4ER01_9BACL Unreviewed; 285 AA.
AC W4ER01;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
DE AltName: Full=PN/PL/PM kinase {ECO:0000256|ARBA:ARBA00042348};
DE AltName: Full=Pyridoxal kinase {ECO:0000256|ARBA:ARBA00042396};
DE AltName: Full=Pyridoxamine kinase {ECO:0000256|ARBA:ARBA00042307};
DE AltName: Full=Vitamin B6 kinase {ECO:0000256|ARBA:ARBA00042531};
GN ORFNames=C176_16962 {ECO:0000313|EMBL:ETT82699.1};
OS Viridibacillus arenosi FSL R5-213.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT82699.1, ECO:0000313|Proteomes:UP000019062};
RN [1] {ECO:0000313|EMBL:ETT82699.1, ECO:0000313|Proteomes:UP000019062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT82699.1,
RC ECO:0000313|Proteomes:UP000019062};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate;
CC Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326;
CC EC=2.7.1.35; Evidence={ECO:0000256|ARBA:ARBA00036247};
CC -!- SIMILARITY: Belongs to the ThiD family.
CC {ECO:0000256|ARBA:ARBA00009879}.
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:ETT82699.1}.
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DR EMBL; ASQA01000034; ETT82699.1; -; Genomic_DNA.
DR RefSeq; WP_051448791.1; NZ_ASQA01000034.1.
DR AlphaFoldDB; W4ER01; -.
DR PATRIC; fig|1227360.4.peg.3453; -.
DR eggNOG; COG0351; Bacteria.
DR Proteomes; UP000019062; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR CDD; cd01169; HMPP_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR PANTHER; PTHR20858:SF19; PYRIDOXINE 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:ETT82699.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019062};
KW Transferase {ECO:0000313|EMBL:ETT82699.1}.
FT DOMAIN 15..256
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 285 AA; 30493 MW; 0738DDA9EC4C924C CRC64;
MTVSRALTIA GSAARGGAGI QADIKTFQEL DVFGTSAITA IVAKNPHTGQ GIFPQSVEAI
EAQIHTILED IGADAIKTGM LFTHEIIINV VKWIQRSGVK KIVVDPVMIG KIGSALLKED
AMEAMRTQLI PLATIITPNM PEASYLLDGM ELNSVEDLKV AAKKLHELGP RYVLVKGGRL
EGPAIDVLYD GEQFYLLEAP RFDTIHTNGA GCTYSAAITA GLAKGQAVPE AVIEAKKFIS
AGIRHSFGFK QGVGPTYHAA YGKYGETDCT VTIESSELST NYDER
//
