ID V6IX25_9BACL Unreviewed; 280 AA.
AC V6IX25;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=P343_09135 {ECO:0000313|EMBL:EST11820.1};
OS Sporolactobacillus laevolacticus DSM 442.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST11820.1, ECO:0000313|Proteomes:UP000018296};
RN [1] {ECO:0000313|EMBL:EST11820.1, ECO:0000313|Proteomes:UP000018296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 442 {ECO:0000313|EMBL:EST11820.1,
RC ECO:0000313|Proteomes:UP000018296};
RX PubMed=24371202;
RA Wang H., Wang L., Ju J., Yu B., Ma Y.;
RT "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an Efficient
RT Polymer-Grade D-Lactate Producer from Agricultural Waste Cottonseed as a
RT Nitrogen Source.";
RL Genome Announc. 1:e01100-13(2013).
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:EST11820.1}.
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DR EMBL; AWTC01000008; EST11820.1; -; Genomic_DNA.
DR RefSeq; WP_023510086.1; NZ_AWTC01000008.1.
DR AlphaFoldDB; V6IX25; -.
DR STRING; 1395513.P343_09135; -.
DR PATRIC; fig|1395513.3.peg.1842; -.
DR eggNOG; COG0351; Bacteria.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000018296; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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:EST11820.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018296};
KW Transferase {ECO:0000313|EMBL:EST11820.1}.
FT DOMAIN 14..267
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 280 AA; 29940 MW; BFCAAD3AB0DA2CA3 CRC64;
MSEHFKAMTI AGSDTSGGAG MQADLKTFQE LGVYGMTALT CIVTMDPYKH WSHSVTTLDT
TLLKKQLDTI VVGIGIDAMK TGMLGSPEII RIAADAIEKN NLERTVIDPV MVCKGAEEEL
QPELQPENTS AMLKLLIPKA LVTTPNLYEA ARLTGMQRIT TIDQMKEAAE KIVALGAKNA
LVKGGSRLPD TDQAIDVLYD GKDFHIIADE RVNTPNIHGA GCTYAAAVTA ELAKGNSVLN
AVKVAKSFVT AGIRASFSLN DYTGPTDHSA YKKEIAAKQA
//