ID A0A0B5AWQ4_9BACL Unreviewed; 279 AA.
AC A0A0B5AWQ4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=JMA_31120 {ECO:0000313|EMBL:AJD92429.1};
OS Jeotgalibacillus malaysiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=1508404 {ECO:0000313|EMBL:AJD92429.1, ECO:0000313|Proteomes:UP000031449};
RN [1] {ECO:0000313|EMBL:AJD92429.1, ECO:0000313|Proteomes:UP000031449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D5 {ECO:0000313|EMBL:AJD92429.1,
RC ECO:0000313|Proteomes:UP000031449};
RA Yaakop A.S., Chan K.-G., Goh K.M.;
RT "Complete genome of a marine bacteria Jeotgalibacillus malaysiensis.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP009416; AJD92429.1; -; Genomic_DNA.
DR RefSeq; WP_039811754.1; NZ_CP009416.1.
DR AlphaFoldDB; A0A0B5AWQ4; -.
DR STRING; 1508404.JMA_31120; -.
DR KEGG; jeo:JMA_31120; -.
DR HOGENOM; CLU_020520_0_0_9; -.
DR OrthoDB; 9810880at2; -.
DR BioCyc; JESP1508404:G14D9-12393-MONOMER; -.
DR Proteomes; UP000031449; Chromosome.
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:AJD92429.1};
KW Transferase {ECO:0000313|EMBL:AJD92429.1}.
FT DOMAIN 13..259
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 279 AA; 29632 MW; 4FDE22B90BDCEA8F CRC64;
MSLNKTLTIA GSDTSGGAGI QADLKTFQEH GTYGMTALTT VVTMDPANHW AHNVHPLAID
TLKAQIDTAL STGISALKTG MLGSVEIIET AAQAIDRAET DKVVIDPVMV CKGEDEVLHP
ETVGAMQEHL LPRAMVVTPN LFEAWQLSGV GPIRTIDDMK AAAAKIVEMG AKSVVVKGGK
QLDHDKAVDL FYDGDTFTLL EAEKADTSYN HGAGCTFAAA ITANLANGLE LNEAVSNAKE
FVTSAIHHGW RLNEYVGPVM HGAHSRFGKV TINKETLNA
//
