ID I3TFA9_THEC1 Unreviewed; 451 AA.
AC I3TFA9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AFK51447.1};
GN OrderedLocusNames=TCELL_1024 {ECO:0000313|EMBL:AFK51447.1};
OS Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermogladius.
OX NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK51447.1, ECO:0000313|Proteomes:UP000005270};
RN [1] {ECO:0000313|EMBL:AFK51447.1, ECO:0000313|Proteomes:UP000005270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22663 / VKM B-2946 / 1633
RC {ECO:0000313|Proteomes:UP000005270};
RX PubMed=22843584; DOI=10.1128/JB.00894-12;
RA Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A.,
RA Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the hyperthermophilic cellulolytic
RT Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL J. Bacteriol. 194:4446-4447(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003531; AFK51447.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TFA9; -.
DR STRING; 1184251.TCELL_1024; -.
DR KEGG; thg:TCELL_1024; -.
DR eggNOG; arCOG00020; Archaea.
DR eggNOG; arCOG00021; Archaea.
DR HOGENOM; CLU_035788_0_0_2; -.
DR InParanoid; I3TFA9; -.
DR Proteomes; UP000005270; Chromosome.
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:AFK51447.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005270};
KW Transferase {ECO:0000313|EMBL:AFK51447.1}.
FT DOMAIN 16..260
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 451 AA; 47959 MW; 96E2AC360F68F1A0 CRC64;
MTSWRIPVAM TIAGSDSGGG AGVEADLKTF SALGVYGTVV ITSVTAQNTR EVRGVYDLPP
DFVYLQIKTV VEDIRVDAAK TGMLSNPGIV GAVADAVGEF GIRLVVDPVM VAKSGARLLR
DDALEALTRR LLPQALLVTP NASEAGVLAG FPVESVEDAK RAARAIHDKY GVPAVVVKGG
HLKADRVVDV LFYEGDYYLY EAERIESGCL HGAGCSFSAA VTAFLARGLK LPEAVKMARG
FMDYAIKYGV RVGGGHCPVN PMAYLEVPAY KYAAIENVRR AVEALLENQA LVMPYAPEVG
INVVEAPHPL YATSPGDVVG VEGRIVRAGG RLVKVGDVRT GASSHLARLV LALVKRGLKV
RGAVNVRYGE DLVERARRAG LRVVFVDRRL EPPELKSREG GSMEWIAGLA GGEEPDLIYD
VGDVGKEPMV RVLGEDAVDA VTKLLSILKT G
//