ID D7DUV1_METV3 Unreviewed; 558 AA.
AC D7DUV1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ADI36911.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:ADI36911.1};
GN OrderedLocusNames=Mvol_1254 {ECO:0000313|EMBL:ADI36911.1};
OS Methanococcus voltae (strain ATCC BAA-1334 / A3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=456320 {ECO:0000313|EMBL:ADI36911.1, ECO:0000313|Proteomes:UP000007722};
RN [1] {ECO:0000313|EMBL:ADI36911.1, ECO:0000313|Proteomes:UP000007722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1334 / A3 {ECO:0000313|Proteomes:UP000007722};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Whitman W.B., Woyke T.;
RT "Complete sequence of Methanococcus voltae A3.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002057; ADI36911.1; -; Genomic_DNA.
DR AlphaFoldDB; D7DUV1; -.
DR STRING; 456320.Mvol_1254; -.
DR KEGG; mvo:Mvol_1254; -.
DR eggNOG; arCOG00020; Archaea.
DR eggNOG; arCOG00021; Archaea.
DR HOGENOM; CLU_035788_0_0_2; -.
DR InParanoid; D7DUV1; -.
DR OrthoDB; 43786at2157; -.
DR Proteomes; UP000007722; 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 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; 2.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADI36911.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007722};
KW Transferase {ECO:0000313|EMBL:ADI36911.1}.
FT DOMAIN 11..235
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT COILED 396..423
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 558 AA; 64247 MW; 8549357A0B193C9F CRC64;
MKNVLAIGGY DPTGGAGVIA DAKTIKETGN NPLTIITSLV PQNNNKVYSK EEISKEILEE
QFQAVFEDFN IKWVKTGVLS KHAIELILEY HKDYDFKIIC DPIIKSTTGQ LLTDKETLDL
YVELFSKCYL ITPNYEEFKF IKHFMYNKLK KEKYYDENLK ELSVLVTGIN DTLQKYSGTK
IAIFNGKKIN REVHGTGCVF ASAIAGFSTR MPIISAIKNA KKLVLGSVIY AKKTRYGYNT
NPIFINEKTI YKNLEYSLFL LNNIKYTLIP DVGSNIAECT ILPKNRYDVC ALSGRIIKDK
HTGGYHRAGE FKFGASKILS DVILTANKYD PKIRSSMGVR FNEKLMEKLK DDGIFCIGHF
DTKKLDNIRK VGFGIDNAFK SHLLDKYKQF MEKDHMHNLE NSFRNAEENV DNLKIDEEDL
KINKINKIKE EVDNISNILT KNLLDKSGHF LHNEKIINET LINSSEEINV EKNKLDVEIE
DECTKISPEE YRKCNNCEYC KNEIIHNFIK FKEGYDFTLD MIYHKGGHQI EPTIWILGQN
SIEIVKKLRI LEKTYRKL
//
