ID A8AAW8_IGNH4 Unreviewed; 430 AA.
AC A8AAW8;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Phosphomethylpyrimidine kinase type-1 {ECO:0000313|EMBL:ABU82070.1};
GN OrderedLocusNames=Igni_0888 {ECO:0000313|EMBL:ABU82070.1};
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591 {ECO:0000313|EMBL:ABU82070.1, ECO:0000313|Proteomes:UP000000262};
RN [1] {ECO:0000313|EMBL:ABU82070.1, ECO:0000313|Proteomes:UP000000262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125
RC {ECO:0000313|Proteomes:UP000000262};
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H.Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU82070.1; -; Genomic_DNA.
DR AlphaFoldDB; A8AAW8; -.
DR STRING; 453591.Igni_0888; -.
DR KEGG; iho:Igni_0888; -.
DR eggNOG; arCOG00020; Archaea.
DR HOGENOM; CLU_035788_0_0_2; -.
DR PhylomeDB; A8AAW8; -.
DR Proteomes; UP000000262; 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 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:ABU82070.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000262};
KW Transferase {ECO:0000313|EMBL:ABU82070.1}.
FT DOMAIN 13..230
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 430 AA; 47133 MW; 8042F79B21A790C4 CRC64;
MNVKKVAAVG GLDPSGGAGI EMDVKVGSAV GVHVHPVATA ITYQTPTEFY GSKCTDIEVL
EGQLKAVKGV RNWKLGMLCN ERIAETLLKY LEGVVVVDPV LKATAGGTLY EGSLETYKKI
LSVSFAVTPN ALEAEALTGL RVRTVDDAIR AAEALAEAGP KLVVITGGHL EIFADVIYYD
GYVEVIRGTR KVTSFHGSGS FMAMALASYL ALGEAPVVAA RKAVGYTRVA HLFSQGKEAL
DPLYQMRYDA VRHCMYEEYK YFIEWLESLP FEKAKKIAPE VGINVAYSVP KELVRGKGSV
LGVPGRLRLT PRGLRSCCNP WWGQADHTAR LLLEAQKYNP KLRVAMNIRY SPENVAALSG
AGYEVYELKR ETEPPGEESM RWAAKKAYSD LGKVPDVIYD KGFYGKEAMI RLLTEGLEEL
KEMLRVVLQI
//