ID U7NVU8_9GAMM Unreviewed; 281 AA.
AC U7NVU8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Pyridoxamine kinase/Phosphomethylpyrimidine kinase domain-containing protein {ECO:0000259|Pfam:PF08543};
GN ORFNames=Q671_08665 {ECO:0000313|EMBL:ERS86495.1};
OS Halomonas sp. PBN3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1397528 {ECO:0000313|EMBL:ERS86495.1, ECO:0000313|Proteomes:UP000017115};
RN [1] {ECO:0000313|EMBL:ERS86495.1, ECO:0000313|Proteomes:UP000017115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBN3 {ECO:0000313|EMBL:ERS86495.1,
RC ECO:0000313|Proteomes:UP000017115};
RX PubMed=24356826;
RA Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA Kostka J.E.;
RT "Draft genome sequences for oil-degrading bacterial strains from beach
RT sands impacted by the deepwater horizon oil spill.";
RL Genome Announc. 1:e01015-13(2013).
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 -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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:ERS86495.1}.
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DR EMBL; AXCA01000166; ERS86495.1; -; Genomic_DNA.
DR RefSeq; WP_023006388.1; NZ_AXCA01000166.1.
DR AlphaFoldDB; U7NVU8; -.
DR PATRIC; fig|1397528.3.peg.2187; -.
DR eggNOG; COG0351; Bacteria.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000017115; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01169; HMPP_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
FT DOMAIN 21..259
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 281 AA; 29305 MW; E45FFC3941049529 CRC64;
MAGEAALEPH LPTVLVLAGH DPTGGAGLVA DAEAVAAAGG WALTVPTALT VQSCRDVAAV
VPADPALMRQ SVAALDEFAV AAIKVGLVAD LATLDAVTDI LGRFPGVPVV ADPVLRAGGG
RELSTIELVD AYRERLLPRV DILTPNRGEL ARLSPGLEED TERAVALMQL GCQGVLVTAT
DDPVPGTPQG RVAHTLHTPD QSRQWSWPRL DGRFHGSGCT LASCLAARLA AGESLVAACE
QAQAFTWEAL AHGWRPGQAQ RLPRRLWRLP GLSPHAAPAS R
//
