ID A0A0R2NVL7_9LACO Unreviewed; 273 AA. AC A0A0R2NVL7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 06-JUL-2016, entry version 7. DE RecName: Full=Pyridoxal kinase {ECO:0000256|SAAS:SAAS00384426}; DE EC=2.7.1.35 {ECO:0000256|SAAS:SAAS00384426}; GN ORFNames=DY78_GL002076 {ECO:0000313|EMBL:KRO28722.1}; OS Lactobacillus fabifermentans DSM 21115. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1413187 {ECO:0000313|EMBL:KRO28722.1, ECO:0000313|Proteomes:UP000050920}; RN [1] {ECO:0000313|EMBL:KRO28722.1, ECO:0000313|Proteomes:UP000050920} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21115 {ECO:0000313|EMBL:KRO28722.1, RC ECO:0000313|Proteomes:UP000050920}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'- CC phosphate. {ECO:0000256|SAAS:SAAS00384372}. CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxal 5'-phosphate from pyridoxal: step 1/1. CC {ECO:0000256|SAAS:SAAS00532463}. CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. CC {ECO:0000256|SAAS:SAAS00571270}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO28722.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AYGX02000033; KRO28722.1; -; Genomic_DNA. DR RefSeq; WP_024626109.1; NZ_AYGX02000033.1. DR UniPathway; UPA01068; UER00298. DR Proteomes; UP000050920; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro. 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 PANTHER; PTHR10534; PTHR10534; 1. DR Pfam; PF08543; Phos_pyr_kin; 1. DR SUPFAM; SSF53613; SSF53613; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00440402}; KW Complete proteome {ECO:0000313|Proteomes:UP000050920}; KW Kinase {ECO:0000256|SAAS:SAAS00440394, ECO:0000313|EMBL:KRO28722.1}; KW Magnesium {ECO:0000256|SAAS:SAAS00532466}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00440335}; KW Transferase {ECO:0000256|SAAS:SAAS00440315}. FT DOMAIN 67 248 Phos_pyr_kin. {ECO:0000259|Pfam:PF08543}. SQ SEQUENCE 273 AA; 28901 MW; 926CB95B1F10C5B0 CRC64; MTKMLVAEDL SAVGGISLSA ALPVLTAMRY QVAALPTSLL STHTSGYGRP AIQDLSTWLP AVFDHWMAAK LDFDQALIGY VGSVELVDLL HKYLMAQQVA LTVVDPVLGD LGELYSGFDG DYVMAMRRLI QTADVILPNV TEASLLTGLP YAADPDLAVL LPALQKLVKP GAHAIITDVT RDDLIGCAWL ADGQVQYSGQ PRLPGHYNGT GDTLAAVIAG LLGQGYSLAQ AVPLANQWLN AAVAETLAEN RDDERQGVAL GNLLRAILAL QAS //