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Database: UniProt
Entry: G6FQ55_9CYAN
LinkDB: G6FQ55_9CYAN
Original site: G6FQ55_9CYAN 
ID   G6FQ55_9CYAN            Unreviewed;       276 AA.
AC   G6FQ55;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:EHC17940.1};
DE            EC=2.7.4.7 {ECO:0000313|EMBL:EHC17940.1};
GN   ORFNames=FJSC11DRAFT_1002 {ECO:0000313|EMBL:EHC17940.1};
OS   Fischerella thermalis JSC-11.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Fischerella.
OX   NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC17940.1, ECO:0000313|Proteomes:UP000004344};
RN   [1] {ECO:0000313|EMBL:EHC17940.1, ECO:0000313|Proteomes:UP000004344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-11 {ECO:0000313|EMBL:EHC17940.1,
RC   ECO:0000313|Proteomes:UP000004344};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA   Woyke T.J.;
RT   "The draft genome of Fischerella sp. JSC-11.";
RL   Submitted (SEP-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.
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:EHC17940.1}.
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DR   EMBL; AGIZ01000003; EHC17940.1; -; Genomic_DNA.
DR   RefSeq; WP_009455282.1; NZ_AGIZ01000003.1.
DR   AlphaFoldDB; G6FQ55; -.
DR   GeneID; 60765206; -.
DR   PATRIC; fig|741277.3.peg.1176; -.
DR   Proteomes; UP000004344; Unassembled WGS sequence.
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: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   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EHC17940.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004344};
KW   Transferase {ECO:0000313|EMBL:EHC17940.1}.
FT   DOMAIN          19..264
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   276 AA;  29024 MW;  29B44F57B18E9E11 CRC64;
     MNAETTSRIP VALTIAGSDS GGGAGIQADL RTFAFHCVHG TSAITCVTAQ NTLGVTRVDA
     IPPEAVIAQM QAVCEDIGVQ AAKTGMLLNK EIIAAVAQQV EALQIHNLVV DPVMVSRAGA
     QLIDDEAVNT LCHTLIPLAA IATPNRYEAQ ILSGLEINTL DDMRKCAQII HEKFKAKVVL
     VKGGGMSGSG RGVDVWFDGQ KLETLSVKQV ETKNTHGTGC TLSAAIAANL ARGDDLFTAV
     QQAKEYVTNA LSYALNIGQG QGPVGHFYPL LLTTNY
//
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