ID B6XX42_9BIFI Unreviewed; 291 AA.
AC B6XX42;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Putative pyridoxal kinase {ECO:0000313|EMBL:EEB20821.1};
GN ORFNames=BIFCAT_01907 {ECO:0000313|EMBL:EEB20821.1};
OS Bifidobacterium catenulatum DSM 16992 = JCM 1194 = LMG 11043.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=566552 {ECO:0000313|EMBL:EEB20821.1};
RN [1] {ECO:0000313|EMBL:EEB20821.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB20821.1};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bifidobacterium catenulatum (DSM 16992).";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB20821.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB20821.1};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000565};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
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:EEB20821.1}.
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; ABXY01000026; EEB20821.1; -; Genomic_DNA.
DR RefSeq; WP_003836592.1; NZ_JGYT01000001.1.
DR AlphaFoldDB; B6XX42; -.
DR GeneID; 45582519; -.
DR KEGG; bcat:BBCT_0601; -.
DR PATRIC; fig|566552.18.peg.629; -.
DR eggNOG; COG2240; Bacteria.
DR Proteomes; UP000003882; Unassembled WGS sequence.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EEB20821.1};
KW Transferase {ECO:0000313|EMBL:EEB20821.1}.
FT DOMAIN 35..265
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 291 AA; 31607 MW; 2C3B1916AA6C15A8 CRC64;
MDDVILYDRD PHYIPRVAAV HDMCGYGNCS LTAAIPILSA AGCDVCPVPT ALFSAHTRYS
VFTFHDTTEI LDGYLDAWRK ENVDLDGVYS GFLGSAEQVA IIKRLYSQYP HALRLVDPVM
GDGGEIYATY TPELCEAMGT LVDGADVLMP NLTEASILTK RTYPGRDLSD AEVDDMIDAL
LDLGAKNVVL KGIDHDDGTI RNYVASADSG ASGKQELAHS KLPFMTHGTG DAFASALCGA
LMAGRPLAES AHIAGEFVRH AMENTQYQPH HDERGVSFEL NLDELTQLVR H
//
