ID   D2RIG3_ACIFV            Unreviewed;       274 AA.
AC   D2RIG3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   OrderedLocusNames=Acfer_0462 {ECO:0000313|EMBL:ADB46865.1};
OS   Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS   106432 / VR4).
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Acidaminococcus.
OX   NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB46865.1, ECO:0000313|Proteomes:UP000001902};
RN   [1] {ECO:0000313|EMBL:ADB46865.1, ECO:0000313|Proteomes:UP000001902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4
RC   {ECO:0000313|Proteomes:UP000001902};
RX   PubMed=21304687; DOI=10.4056/sigs.1002553;
RA   Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acidaminococcus fermentans type strain
RT   (VR4).";
RL   Stand. Genomic Sci. 3:1-14(2010).
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}.
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DR   EMBL; CP001859; ADB46865.1; -; Genomic_DNA.
DR   RefSeq; WP_012937855.1; NZ_CP085936.1.
DR   AlphaFoldDB; D2RIG3; -.
DR   STRING; 591001.Acfer_0462; -.
DR   GeneID; 78334219; -.
DR   KEGG; afn:Acfer_0462; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_0_9; -.
DR   OrthoDB; 9810880at2; -.
DR   Proteomes; UP000001902; Chromosome.
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:0000313|EMBL:ADB46865.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001902};
KW   Transferase {ECO:0000313|EMBL:ADB46865.1}.
FT   DOMAIN          11..259
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   274 AA;  28928 MW;  AE6EDDFDC99FECC0 CRC64;
     MFHLLTIAGS DSSGGAGIQA DLKTFAAHGC YGMSVITAVT AQNTTGVTAI QNIDPEVVEA
     QIDAVFQDIR VDGVKVGMVS NSALIRAIAK KMQQYAPPVL VVDPVMVATS GSYLLEKEAR
     KDLQEKLLPL ATLITPNMQE GEALSGLSIH SREDMEKAAA VICQKGARAV LLKGGHLAET
     ADDYLLYPGE GNWLQGKWFP GQRFANPNTH GTGCSLSSAL ASEMAAGASL PEAVEKAKAY
     VALGIQHGLA VGHGHGPIHH FVDLYRKAGW EEGK
//