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Database: UniProt
Entry: I9B294_9FIRM
LinkDB: I9B294_9FIRM
Original site: I9B294_9FIRM 
ID   I9B294_9FIRM            Unreviewed;       287 AA.
AC   I9B294;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=FB4_2982 {ECO:0000313|EMBL:EIW19272.1};
OS   Pelosinus fermentans B4.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW19272.1, ECO:0000313|Proteomes:UP000004324};
RN   [1] {ECO:0000313|EMBL:EIW19272.1, ECO:0000313|Proteomes:UP000004324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:EIW19272.1,
RC   ECO:0000313|Proteomes:UP000004324};
RX   PubMed=22933770; DOI=10.1128/JB.01174-12;
RA   Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA   Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA   Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT   "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT   Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL   J. Bacteriol. 194:5147-5148(2012).
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:EIW19272.1}.
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DR   EMBL; AKVJ01000021; EIW19272.1; -; Genomic_DNA.
DR   RefSeq; WP_007932855.1; NZ_AKVJ01000021.1.
DR   AlphaFoldDB; I9B294; -.
DR   PATRIC; fig|1149862.3.peg.1538; -.
DR   OrthoDB; 9800808at2; -.
DR   Proteomes; UP000004324; 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:EIW19272.1};
KW   Transferase {ECO:0000313|EMBL:EIW19272.1}.
FT   DOMAIN          73..252
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   287 AA;  31793 MW;  517613B50C60C31A CRC64;
     MKQKLARVVA IHDMSGYGKC SLTVAIPVIS AAGIEVCPLP TALLSTNTLF PGFKFFDFTP
     QMNEFINHWK EIDFKTDCAY SGFLGSAEQI QIVKNFMLDF KCSLKIVDPV MGDNGIIIKT
     YTPEMCSTMR ELASIADIVT PNLTEAYILT GRDYIDGEID SDTSRKLCAQ IIEMGAKNIV
     LTGVVRGNSL YNCAMSEDHS YFEAAVDLLP YHMHGTGDLF TSVLTAGVVN GYTLKESVES
     AAHFVRDAMI VSNDIEDAFD RGVAFEPIVY KLRSGLYNKI WLKKERA
//
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