ID A0A1B8Q9I1_9GAMM Unreviewed; 265 AA.
AC A0A1B8Q9I1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:OBX75438.1};
GN ORFNames=A9306_02585 {ECO:0000313|EMBL:OBX75438.1};
OS Moraxella atlantae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=34059 {ECO:0000313|EMBL:OBX75438.1, ECO:0000313|Proteomes:UP000092616};
RN [1] {ECO:0000313|EMBL:OBX75438.1, ECO:0000313|Proteomes:UP000092616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 59586 {ECO:0000313|EMBL:OBX75438.1,
RC ECO:0000313|Proteomes:UP000092616};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome of Moraxella atlantae CCUG 59586.";
RL Submitted (JUN-2016) 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 -!- 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:OBX75438.1}.
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DR EMBL; LZNA01000070; OBX75438.1; -; Genomic_DNA.
DR RefSeq; WP_067338913.1; NZ_LZNA01000070.1.
DR AlphaFoldDB; A0A1B8Q9I1; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000092616; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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;
KW Kinase {ECO:0000313|EMBL:OBX75438.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092616};
KW Transferase {ECO:0000313|EMBL:OBX75438.1}.
FT DOMAIN 12..247
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 265 AA; 28241 MW; 2666FDE1CDCA56DF CRC64;
MRPTVLCFSG LDPSGGAGLQ ADIEAIGQSG AHAAVICTAL TVQSSQQVYG FEPCNRALLH
QQTQTVLADL PVRAVKSGML GTTDNIALLA ELFASGAIAH GTPYVLDPVL VANSGGALGD
KTTLVTAFSQ LLPFATLATP NSHELRDLTG IDALDKAARD LCQRGCHAVL VKTAHENHDA
AIEQTLYARD AEAVRLVYRT RLPRLTGEYH GSGCSLASYV AGRLAMGDHL AVAMQCADIW
EQQVLRAADI PHTDGQRIPK RFWYI
//
