ID A0A372IZV6_9ACTN Unreviewed; 283 AA.
AC A0A372IZV6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Pyridoxal kinase PdxY {ECO:0000313|EMBL:RFU20428.1};
DE EC=2.7.1.35 {ECO:0000313|EMBL:RFU20428.1};
GN Name=pdxY {ECO:0000313|EMBL:RFU20428.1};
GN ORFNames=D0Z06_16235 {ECO:0000313|EMBL:RFU20428.1};
OS Geodermatophilus sp. LHW52908.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2303986 {ECO:0000313|EMBL:RFU20428.1, ECO:0000313|Proteomes:UP000262362};
RN [1] {ECO:0000313|EMBL:RFU20428.1, ECO:0000313|Proteomes:UP000262362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW52908 {ECO:0000313|EMBL:RFU20428.1,
RC ECO:0000313|Proteomes:UP000262362};
RA Li L., Lin H.W.;
RT "Geodermatophilus marinus sp. nov., isolated from marine sponge Leucetta
RT chagosensis.";
RL Submitted (AUG-2018) 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:RFU20428.1}.
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DR EMBL; QVQH01000015; RFU20428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372IZV6; -.
DR OrthoDB; 9800808at2; -.
DR Proteomes; UP000262362; 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 NCBIfam; TIGR00687; pyridox_kin; 1.
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:RFU20428.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000262362};
KW Transferase {ECO:0000313|EMBL:RFU20428.1}.
FT DOMAIN 76..258
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 283 AA; 29611 MW; B7CFB00781FAC335 CRC64;
MVAVLSVQSH VAYGHVGNSS AVFPLQRLGI EVWPVHTVQF SNHTGYGAWR GRVFDGPAIE
EVVDGIAERG VLGGADAVLS GYLGSADIGH AVVGTVRRVQ EANPAAVYCC DPVTGDVGRG
VFVRPGIPEF MREVAVPAAD VVTPNHFELD LLAGAETRSL ASVRDAVAAV QALGPRVVLT
TSLVTDDTPD GAVDLLASEG GRHHRVRTPR LGVSVNGAGD AIAALFLAHW LDTRDAGTAL
ERAAASVYGL LKATEDAGSR EILLVEAQEE VVTPSRTFPV EEV
//