ID G7VII8_9CREN Unreviewed; 449 AA.
AC G7VII8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AET33468.1};
GN ORFNames=P186_2074 {ECO:0000313|EMBL:AET33468.1};
OS Pyrobaculum ferrireducens.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET33468.1, ECO:0000313|Proteomes:UP000005867};
RN [1] {ECO:0000313|EMBL:AET33468.1, ECO:0000313|Proteomes:UP000005867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1860 {ECO:0000313|EMBL:AET33468.1,
RC ECO:0000313|Proteomes:UP000005867};
RX PubMed=22247528; DOI=10.1128/JB.06465-11;
RA Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT pyrobaculum able to grow with various electron acceptors.";
RL J. Bacteriol. 194:727-728(2012).
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DR EMBL; CP003098; AET33468.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VII8; -.
DR STRING; 1104324.P186_2074; -.
DR KEGG; pyr:P186_2074; -.
DR eggNOG; arCOG00020; Archaea.
DR HOGENOM; CLU_035788_0_0_2; -.
DR OrthoDB; 43786at2157; -.
DR BioCyc; PSP1104324:GJSN-2024-MONOMER; -.
DR Proteomes; UP000005867; 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:AET33468.1};
KW Transferase {ECO:0000313|EMBL:AET33468.1}.
FT DOMAIN 12..256
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 449 AA; 48190 MW; 2687DF96E58BBBA2 CRC64;
MWRVAITIAG LDSGGGAGIH ADVKTFAAMG VHGATALTCV TAQNTYEVRE VQCLSPAMVR
AQILAVWDDM GIDAGKTGML GTGEIIEEVA ATVEKLGFPL VVDPVMVAKS GAPLISDDAV
DVLKKRLLPV AKVATPNRPE AERLTGMSIA SERDAERAAE YIHREYGTEV VIVKGGHLPG
GEAVDVVYYR GAVHKFSTPR LDSRATHGTG CAYSAAIAAG LAKGLDPLEA VKTAKQFIYT
AIKYGVARGK GHWAVNPTAW VEIPAERWRA VEELEAALKL VRRNAERLAK AIPEVQSNLG
YVIDPRYARD TGDVAAVPGR IVNYMGEARP SGPPTFGASS HVARKILALA SRDPRARSAM
NIRYDPELVE RAKALGFKIA VVDRRREPEE VKKREGGTMQ WVVEEALRQT GGVAPDLIVD
LGDWGKEPQI TVVGKTPAEV VEKVLKILS
//
