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Database: UniProt
Entry: V6IX25_9BACL
LinkDB: V6IX25_9BACL
Original site: V6IX25_9BACL 
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
//
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