ID   S3MSD2_9GAMM            Unreviewed;       256 AA.
AC   S3MSD2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:EPF70735.1};
GN   ORFNames=F945_02979 {ECO:0000313|EMBL:EPF70735.1};
OS   Acinetobacter rudis CIP 110305.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF70735.1, ECO:0000313|Proteomes:UP000014568};
RN   [1] {ECO:0000313|EMBL:EPF70735.1, ECO:0000313|Proteomes:UP000014568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF70735.1,
RC   ECO:0000313|Proteomes:UP000014568};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL   Submitted (JUN-2013) 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:EPF70735.1}.
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DR   EMBL; ATGI01000036; EPF70735.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3MSD2; -.
DR   STRING; 632955.GCA_000829675_03300; -.
DR   PATRIC; fig|421052.3.peg.2910; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_2_6; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000014568; 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:EPF70735.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014568};
KW   Transferase {ECO:0000313|EMBL:EPF70735.1}.
FT   DOMAIN          13..243
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   256 AA;  26915 MW;  F4006356B7A72D9A CRC64;
     MVRATVLCFS GLDPSGGAGI QADIESIGQS GAHAAIACTA LTIQNSQQVF GFEAASKQLL
     LAQANAVVKD LPIRCVKSGM LGTTENIAAL AEFLAEHPDY QYVLDPVLVA NSGGSLGNQA
     TFVKAFAELI PLATVITPNT VELRALTGED DLELATQKLF AMGAQAILVK GGHEDTPDYI
     RNALYIAGEL VAESRCPRLA GEYHGSGCSL ASFIAGRLAQ GDALKTAVQH AETWLFGVLQ
     QAESPVENGQ KMPKRF
//