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Database: UniProt
Entry: F7KRI5_9FIRM
LinkDB: F7KRI5_9FIRM
Original site: F7KRI5_9FIRM 
ID   F7KRI5_9FIRM            Unreviewed;       281 AA.
AC   F7KRI5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000256|ARBA:ARBA00019161};
DE            EC=2.7.1.49 {ECO:0000256|ARBA:ARBA00012135};
DE            EC=2.7.4.7 {ECO:0000256|ARBA:ARBA00012963};
DE   AltName: Full=Hydroxymethylpyrimidine kinase {ECO:0000256|ARBA:ARBA00042102};
DE   AltName: Full=Hydroxymethylpyrimidine phosphate kinase {ECO:0000256|ARBA:ARBA00043176};
GN   ORFNames=HMPREF0993_01580 {ECO:0000313|EMBL:EGN39333.1};
OS   Lachnospiraceae bacterium 5_1_57FAA.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658085 {ECO:0000313|EMBL:EGN39333.1, ECO:0000313|Proteomes:UP000005617};
RN   [1] {ECO:0000313|EMBL:EGN39333.1, ECO:0000313|Proteomes:UP000005617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5_1_57FAA {ECO:0000313|EMBL:EGN39333.1,
RC   ECO:0000313|Proteomes:UP000005617};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 5_1_57FAA.";
RL   Submitted (MAY-2011) 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; 4-
CC       amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole: step 2/3. {ECO:0000256|ARBA:ARBA00037917}.
CC   -!- SIMILARITY: Belongs to the ThiD family.
CC       {ECO:0000256|ARBA:ARBA00009879}.
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:EGN39333.1}.
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DR   EMBL; ACTR01000011; EGN39333.1; -; Genomic_DNA.
DR   RefSeq; WP_009248714.1; NZ_AP024846.1.
DR   AlphaFoldDB; F7KRI5; -.
DR   GeneID; 69693122; -.
DR   PATRIC; fig|658085.3.peg.1629; -.
DR   HOGENOM; CLU_020520_0_1_9; -.
DR   Proteomes; UP000005617; 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   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   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGN39333.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005617};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGN39333.1}.
FT   DOMAIN          11..254
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   281 AA;  29668 MW;  21E95B32171226C7 CRC64;
     MRTALTIAGS DSSGGAGIQA DIKTMIANGV YAMSAITALT AQNTTGVTGI MEVTPEFLAE
     QLDDIFTDIY PDAVKIGMVS ASPLIRIIAE KLKAYKADKI VVDPVMVATS GSRLISDEAI
     ETLKECLLPM ASVLTPNIPE AEVLSGLAIE TQKDMVAAAG AISRTYSCAV LLKGGHQIND
     ANDLLYREDS YKWFNGRRID NPNTHGTGCT LSSAIASNLA KGFDLDTSVE RAKAYISGAL
     GAMLDLGRGS GPMDHGFALT GEFIREKEER IAPDSNKGEA C
//
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