ID A0A0M0G0S8_9BACI Unreviewed; 269 AA.
AC A0A0M0G0S8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AF331_19715 {ECO:0000313|EMBL:KON83066.1};
OS Rossellomorea marisflavi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189381 {ECO:0000313|EMBL:KON83066.1, ECO:0000313|Proteomes:UP000037405};
RN [1] {ECO:0000313|Proteomes:UP000037405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14235 jcm11544.";
RL Submitted (JUL-2015) 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}.
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:KON83066.1}.
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DR EMBL; LGUE01000008; KON83066.1; -; Genomic_DNA.
DR RefSeq; WP_053429694.1; NZ_LGUE01000008.1.
DR AlphaFoldDB; A0A0M0G0S8; -.
DR STRING; 189381.GCA_900166615_00276; -.
DR GeneID; 42294165; -.
DR PATRIC; fig|189381.12.peg.3471; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000037405; 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:KON83066.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037405};
KW Transferase {ECO:0000313|EMBL:KON83066.1}.
FT DOMAIN 13..259
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 269 AA; 29009 MW; 265EF30659CCB168 CRC64;
MTLKKTLTIA GSDTSGGAGI QADLKTFQEH GVYGMTALTT VVTMDPADHW HHNVHPLPVS
TLEAQLETVL SVGIDAMKTG MLGTVEVIEL AAKKIDQYGL NKVVIDPVMV CKGEDEVLHP
ETTDAMREHL LQRATVVTPN LFEAGQLAQS GPIKTIEGMK EAAKKIHDLG AKNVVIKGGK
QLEHTKALDL FYDGTDFTIL EEDKVDTTYN HGAGCTFAAA ITANLANGQD VKEAVTNAKI
FVTAAIKHGF KLNEYVGPVM HGAYNRFEK
//