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Database: UniProt
Entry: A0A132PN85_9MYCO
LinkDB: A0A132PN85_9MYCO
Original site: A0A132PN85_9MYCO 
ID   A0A132PN85_9MYCO        Unreviewed;       278 AA.
AC   A0A132PN85;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:KWX23796.1, ECO:0000313|EMBL:ORX11252.1};
GN   ORFNames=AFM11_13590 {ECO:0000313|EMBL:KWX23796.1}, AWC31_03835
GN   {ECO:0000313|EMBL:ORX11252.1};
OS   Mycolicibacterium wolinskyi.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX23796.1, ECO:0000313|Proteomes:UP000070612};
RN   [1] {ECO:0000313|EMBL:KWX23796.1, ECO:0000313|Proteomes:UP000070612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC_01 {ECO:0000313|EMBL:KWX23796.1,
RC   ECO:0000313|Proteomes:UP000070612};
RA   de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA   Limbago B.M., Noble-Wang J.;
RT   "A draft genome sequence of Mycobacterium wolinskyi.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORX11252.1, ECO:0000313|Proteomes:UP000193964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700010 {ECO:0000313|EMBL:ORX11252.1,
RC   ECO:0000313|Proteomes:UP000193964};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) 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:KWX23796.1}.
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DR   EMBL; LGTW01000007; KWX23796.1; -; Genomic_DNA.
DR   EMBL; LQQA01000031; ORX11252.1; -; Genomic_DNA.
DR   RefSeq; WP_067849442.1; NZ_LQQA01000031.1.
DR   AlphaFoldDB; A0A132PN85; -.
DR   STRING; 59750.AWC31_03835; -.
DR   PATRIC; fig|59750.3.peg.6814; -.
DR   OrthoDB; 34166at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000070612; Unassembled WGS sequence.
DR   Proteomes; UP000193964; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   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   Kinase {ECO:0000313|EMBL:KWX23796.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070612};
KW   Transferase {ECO:0000313|EMBL:KWX23796.1}.
FT   DOMAIN          23..271
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   278 AA;  28794 MW;  10B3E150E3ABB6D2 CRC64;
     MNYLSLPPAG HTPLRVMTIA GSDSGGGAGI QADMRTFAML GLHGCVALTA VTVQNSVGVK
     GFHEIPLDVV AGQISAVTSD IGIQAAKTGM LASSDIISTI AETWRGEGLA GQVPLVVDPV
     CASMHGDPLL HPSALDALRT DLFPLATLVT PNLDEVRLLV DIEVVDPASQ KEAARALHAL
     GPQWALVKGG HLRSSAASPD ILFNGSDFYE FDAPRVDTGH DHGAGDTLAA ATACALAHGY
     SVPDAVEFGK AWVTECIRAA YPLGHGHGPV NALFRLQS
//
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