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Database: UniProt
Entry: A0A1E3QFM4_LIPST
LinkDB: A0A1E3QFM4_LIPST
Original site: A0A1E3QFM4_LIPST 
ID   A0A1E3QFM4_LIPST        Unreviewed;       343 AA.
AC   A0A1E3QFM4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=LIPSTDRAFT_1228 {ECO:0000313|EMBL:ODQ75807.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ75807.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ75807.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ75807.1,
RC   ECO:0000313|Proteomes:UP000094385};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC       {ECO:0000256|ARBA:ARBA00008805}.
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DR   EMBL; KV454290; ODQ75807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3QFM4; -.
DR   STRING; 675824.A0A1E3QFM4; -.
DR   OrthoDB; 5472295at2759; -.
DR   Proteomes; UP000094385; Unassembled WGS sequence.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR   CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlKinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; TIGR00687; pyridox_kin; 1.
DR   PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR   PANTHER; PTHR10534:SF2; PYRIDOXAL KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000094385}.
FT   DOMAIN          113..235
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   343 AA;  38310 MW;  20D1E5483CB23641 CRC64;
     MADAKRVLAV SSHVVHGYVG NRASTLPLQL LYWDVDVLNT VSFSNHTGYT QWRGDRHSAQ
     HIREIYTGLK MNTLTDYDVV VTGYIPGAEA VREVGAVVQE LRRDNAELGR EVLWILDPVM
     GDEEKLYVAP DVIPVYESLL PLATVITPNQ FEAELLSGIK FQSAPDIKTA LCTLYDKFGT
     PNIVISSAVA ADDAKKEEFV CAGQTRRKDG SLLQFYLRLP FINAYFTGTG DLFASLMSDR
     FWTYYTAAKG ADGDVPDAEL PLVRAVEDVS AIVQAVLRNT ADEVQKYNIR EDKMAAETGI
     PRPEPGTKER RIRDMKFGEL RLIQSQDKIR VPEVVVKARF DFA
//
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