ID R6I8L9_9FIRM Unreviewed; 283 AA.
AC R6I8L9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=BN517_01023 {ECO:0000313|EMBL:CDB42839.1};
OS Ruminococcus sp. CAG:177.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262952 {ECO:0000313|EMBL:CDB42839.1, ECO:0000313|Proteomes:UP000018315};
RN [1] {ECO:0000313|EMBL:CDB42839.1, ECO:0000313|Proteomes:UP000018315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:177 {ECO:0000313|Proteomes:UP000018315};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDB42839.1}.
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DR EMBL; CBDQ010000149; CDB42839.1; -; Genomic_DNA.
DR AlphaFoldDB; R6I8L9; -.
DR STRING; 1262952.BN517_01023; -.
DR Proteomes; UP000018315; 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:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDB42839.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018315};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDB42839.1}.
FT DOMAIN 73..260
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 283 AA; 30782 MW; EAF9025A95B44CB8 CRC64;
MERLKRAAAI HDISGFGKCS LTVALPIISA MGIEVSVIPT AVLSTHTGGF TGFTYRDLTG
DMRPIAEHWK SLGIKFDAIY SGFLGSVEQI DIVTDFIDDF KEKNTVVLVD PAMADGGKMY
TVFDMDFAKQ MTRLCAKADI IVPNFTEAAF MLGEEYRPAP YSKEYVESTL RRLSCLGPSK
VVLTGVAFDG RQVGSASYDR STDEISYALS DTVDGYFHGT GDVFASALLG AYMNGLSLAE
SARIAVDYTH GCIVRTKEAG TDLRYGVDFE HGIPDLLRQT GII
//
