ID A0A8J4EBF4_9ACTN Unreviewed; 265 AA.
AC A0A8J4EBF4;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Pyridoxamine kinase/Phosphomethylpyrimidine kinase domain-containing protein {ECO:0000259|Pfam:PF08543};
GN ORFNames=Voc01_035680 {ECO:0000313|EMBL:GIJ68651.1};
OS Virgisporangium ochraceum.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Virgisporangium.
OX NCBI_TaxID=65505 {ECO:0000313|EMBL:GIJ68651.1, ECO:0000313|Proteomes:UP000635606};
RN [1] {ECO:0000313|EMBL:GIJ68651.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 16418 {ECO:0000313|EMBL:GIJ68651.1};
RA Komaki H., Tamura T.;
RT "Whole genome shotgun sequence of Virgisporangium ochraceum NBRC 16418.";
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC {ECO:0000256|ARBA:ARBA00003848}.
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; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 3/3. {ECO:0000256|ARBA:ARBA00004769}.
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:GIJ68651.1}.
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DR EMBL; BOPH01000045; GIJ68651.1; -; Genomic_DNA.
DR RefSeq; WP_203928597.1; NZ_BOPH01000045.1.
DR AlphaFoldDB; A0A8J4EBF4; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000635606; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01169; HMPP_kinase; 1.
DR FunFam; 3.40.1190.20:FF:000003; Phosphomethylpyrimidine kinase ThiD; 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 NCBIfam; TIGR00097; HMP-P_kinase; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000635606};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..257
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 265 AA; 27434 MW; F92142245C9CCC1D CRC64;
MTQPVTVLTI AGSDSGGGAG LQADLKAFAL NGVFGTSVVT VLTAQNSAEI RAIEKVPAAF
VQSQLDAVLA DLPVAAVKTG MLASEETVRT VAANVARLPN LVVDPVLVSS DGAKLFPSTV
DRAYVEGLFP HAAVITPNIR EATILTGREI RTDDDLAAAA TDLGRTGARC VVVKGGGRPG
GEAVDAVWHD GTVRFLRSPW VATRNNHGTG CTFAATTAAL LARRVPVQDA LDEAKRYVQA
AIERGAAWQI GAGHGPLGWP TAEDH
//
