ID U1FG34_9ACTN Unreviewed; 345 AA.
AC U1FG34;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Pyridoxal kinase {ECO:0000313|EMBL:ERF58206.1};
DE Flags: Fragment;
GN ORFNames=H641_01396 {ECO:0000313|EMBL:ERF58206.1}, L860_14885
GN {ECO:0000313|EMBL:OCT41753.1};
OS Cutibacterium granulosum DSM 20700.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF58206.1, ECO:0000313|Proteomes:UP000016307};
RN [1] {ECO:0000313|EMBL:ERF58206.1, ECO:0000313|Proteomes:UP000016307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF58206.1,
RC ECO:0000313|Proteomes:UP000016307};
RX PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA Brinkmann V., Meyer T.F., Bruggemann H.;
RT "Comparative genomics reveals distinct host-interacting traits of three
RT major human-associated propionibacteria.";
RL BMC Genomics 14:640-640(2013).
RN [2] {ECO:0000313|EMBL:OCT41753.1, ECO:0000313|Proteomes:UP000094467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:OCT41753.1,
RC ECO:0000313|Proteomes:UP000094467};
RA Jahns A.C., Eilers H., Alexeyev O.A.;
RL Submitted (MAY-2014) 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:ERF58206.1}.
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DR EMBL; AOSS01000038; ERF58206.1; -; Genomic_DNA.
DR EMBL; JNBU01000099; OCT41753.1; -; Genomic_DNA.
DR AlphaFoldDB; U1FG34; -.
DR PATRIC; fig|1160719.4.peg.260; -.
DR OrthoDB; 9800808at2; -.
DR Proteomes; UP000016307; Unassembled WGS sequence.
DR Proteomes; UP000094467; 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; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ERF58206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016307};
KW Transferase {ECO:0000313|EMBL:ERF58206.1}.
FT DOMAIN 61..139
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 145..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ERF58206.1"
SQ SEQUENCE 345 AA; 36034 MW; 150F4E53514776AF CRC64;
GHVGNGAAVF PLQRNGVEVI SLPTAVLSNH NGYPNVGSIP VNAQDLRAVL RSLGHNGFLG
RCDAVLSGYL TETSGPVVVD AVQQIRARGG AGHYLCDPVM GDDGRCYVSD GVVQMMRELV
VPAADIITPN LFELAMLTDH PGLATCPGPT SRPGDTATTS TRGDGNSMPT CAEVIAAARS
LMGSALMGSA RDDAEHHAGT WHVMSHTTDQ NPFRPRASGA TVAGPRAVVV TSVRTTDLPE
DQTHVMTVTP NSAWVCSTPT LSRHFSGSGD LFAALLLAGL LHGQQKNSDA RLSEAVARAT
QQTWLVLSAT ASDAPESEEP GELALVAHQD LLTVQEGAAT RRLAQ
//
