ID U2E1W1_9EURY Unreviewed; 462 AA.
AC U2E1W1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Hydroxymethylpyrimidine phosphate kinase protein {ECO:0000313|EMBL:ERJ06298.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:ERJ06298.1};
GN Name=thiD {ECO:0000313|EMBL:ERJ06298.1};
GN ORFNames=HLRTI_001643 {ECO:0000313|EMBL:ERJ06298.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ06298.1, ECO:0000313|Proteomes:UP000003861};
RN [1] {ECO:0000313|EMBL:ERJ06298.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ06298.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=21705593; DOI=10.1128/JB.05462-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT a deep-sea anoxic brine lake.";
RL J. Bacteriol. 193:4553-4554(2011).
RN [2] {ECO:0000313|EMBL:ERJ06298.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ06298.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
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:ERJ06298.1}.
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DR EMBL; AFNT02000017; ERJ06298.1; -; Genomic_DNA.
DR RefSeq; WP_008524088.1; NZ_AFNT02000017.1.
DR AlphaFoldDB; U2E1W1; -.
DR GeneID; 23798918; -.
DR OrthoDB; 43786at2157; -.
DR Proteomes; UP000003861; Unassembled WGS sequence.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase 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 Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR019293; ThiN.
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 Pfam; PF10120; ThiP_synth; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ERJ06298.1};
KW Transferase {ECO:0000313|EMBL:ERJ06298.1}.
FT DOMAIN 20..261
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 462 AA; 48221 MW; 0170524B2DB03B95 CRC64;
MTRNEAPHEP PAVLTIAGSD SGGGAGIQAD LKTIEAVGGF GTSAITSVTA QNTTGVQGSH
LLPIADIEAQ IQAVLEDFDV RAAKTGMLAT GEVIETVVEY AEDLPALVVD PVMIAASGDR
LLEPDAEDAY EELVAESTLV TPNADEAVVL TGIEPTDEET ALEAGETLVE MGADAALVKG
GHIAGDDVLD VLVTAEDVRT FRHERIDTDA THGSGCTLSA AIATHIAQGE SLADSVSAGI
DLLARAVRYN LDVGEGAGAV HHLVEARERA ARTETAEAVE KLVDDLIDSD VAPLVPDIGT
NVVGATPFAE RIQEVAAVEG RITRTMDGVA PNRGVRFGAS THVARYLLDA REVDATFRFA
TNWRYDDAVA DALDTLNGDV VELDGHPTLE SGVVSALADA EGPVAVVDPG GDGRVPVTIL
LVRDRETLLN RTSQLLDAVD DLVSTDGIQS PSTRSRASRP RR
//
