ID A8G335_PROM2 Unreviewed; 259 AA.
AC A8G335;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ABV50016.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:ABV50016.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:ABV50016.1};
GN Name=thiD {ECO:0000313|EMBL:ABV50016.1};
GN OrderedLocusNames=P9215_04001 {ECO:0000313|EMBL:ABV50016.1};
OS Prochlorococcus marinus (strain MIT 9215).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93060 {ECO:0000313|EMBL:ABV50016.1, ECO:0000313|Proteomes:UP000002014};
RN [1] {ECO:0000313|EMBL:ABV50016.1, ECO:0000313|Proteomes:UP000002014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9215 {ECO:0000313|EMBL:ABV50016.1,
RC ECO:0000313|Proteomes:UP000002014};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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}.
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DR EMBL; CP000825; ABV50016.1; -; Genomic_DNA.
DR RefSeq; WP_012007158.1; NC_009840.1.
DR AlphaFoldDB; A8G335; -.
DR STRING; 93060.P9215_04001; -.
DR KEGG; pmh:P9215_04001; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_3; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000002014; Chromosome.
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: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:ABV50016.1};
KW Transferase {ECO:0000313|EMBL:ABV50016.1}.
FT DOMAIN 13..256
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 259 AA; 27889 MW; CE9BD41BEB642B7B CRC64;
MYSKIALSIG GSDSGGGAGI QADLRTFMAL KVHGCSVVTC ITAQNSFEVA CVEAVEKNTL
LSQLDVLFSD FSIDALKTGM LLNESIIKDT ASKLNTYKIN KIIDPVMVTR TGSKLLEDSA
INAYKKLLLP IADLVTPNIY EANLLSGLEI RNKEDIENSA KIIIGLGAKA VLIKGGGLKD
MKGKDFFLDF NGRKEWFYNN FINTKNTHGS GCTLSAAICG FKALGFDLID SIQKAKLFVE
KSLENSYKIG SGPGPLGHH
//