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Database: UniProt
Entry: G4RPL7_THETK
LinkDB: G4RPL7_THETK
Original site: G4RPL7_THETK 
ID   G4RPL7_THETK            Unreviewed;       450 AA.
AC   G4RPL7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Phosphomethylpyrimidine kinase fused to uncharacterized domain {ECO:0000313|EMBL:CCC81512.1};
DE            EC=2.7.4.7 {ECO:0000313|EMBL:CCC81512.1};
GN   Name=thiD {ECO:0000313|EMBL:CCC81512.1};
GN   OrderedLocusNames=TTX_0857 {ECO:0000313|EMBL:CCC81512.1};
OS   Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS   / Kra 1).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC81512.1, ECO:0000313|Proteomes:UP000002654};
RN   [1] {ECO:0000313|EMBL:CCC81512.1, ECO:0000313|Proteomes:UP000002654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC   {ECO:0000313|Proteomes:UP000002654};
RX   PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA   Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA   Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA   Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA   Hensel R.;
RT   "The complete genome sequence of Thermoproteus tenax: a physiologically
RT   versatile member of the Crenarchaeota.";
RL   PLoS ONE 6:E24222-E24222(2011).
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DR   EMBL; FN869859; CCC81512.1; -; Genomic_DNA.
DR   RefSeq; WP_014126768.1; NC_016070.1.
DR   AlphaFoldDB; G4RPL7; -.
DR   STRING; 768679.TTX_0857; -.
DR   PaxDb; 768679-TTX_0857; -.
DR   GeneID; 11261752; -.
DR   KEGG; ttn:TTX_0857; -.
DR   PATRIC; fig|768679.9.peg.866; -.
DR   eggNOG; arCOG00020; Archaea.
DR   HOGENOM; CLU_035788_0_0_2; -.
DR   OrthoDB; 43786at2157; -.
DR   Proteomes; UP000002654; Chromosome.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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:CCC81512.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002654};
KW   Transferase {ECO:0000313|EMBL:CCC81512.1}.
FT   DOMAIN          13..257
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   450 AA;  49192 MW;  D1F24C526D56CDC8 CRC64;
     MSWRVAMTIA GLDSGGGAGI HADIKTFAAL GVHGTTALTC VTAQNTYEVR AVQCMPREMV
     RSQIMAVWDD MGIDAAKTGM LGTKEIIEEV ADVVSKLGFP LVVDPVMIAK SGAPLISEDA
     MDALSRELLP IAKIVTPNRF EAERLTGMKI SSLEDAKRAA EKIHRELGSD IVIVKGGHLN
     VQDAVDVVYI GGTFHELRTP RLNDRATHGT GCSFSAAIAA GLARGREPLE AIKTAKELIY
     TAIKYGVPKG KGHWPVNPTA WVEIPAERWR VYEVMSQALS LLDRYAELFG PLIPEVQSNL
     GYAIDPRYAE SREDVAAVPG RIVRYMNRAR PSGPPTFGAS DHVARKILAA VRHDPQKRAA
     MNIRFDEGFI ERAKRAGYKV AIIDRRNEPK EVKEKEGGTM QWIVEESVRQ VGGVPDIIVD
     LGDWGKEPMI TVLGKDPEDV IRTIIRIVSS
//
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