ID D2RZQ7_HALTV Unreviewed; 453 AA.
AC D2RZQ7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ADB62096.1};
GN OrderedLocusNames=Htur_3232 {ECO:0000313|EMBL:ADB62096.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB62096.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB62096.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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; CP001860; ADB62096.1; -; Genomic_DNA.
DR RefSeq; WP_012944355.1; NC_013743.1.
DR AlphaFoldDB; D2RZQ7; -.
DR STRING; 543526.Htur_3232; -.
DR GeneID; 8743852; -.
DR KEGG; htu:Htur_3232; -.
DR eggNOG; arCOG00020; Archaea.
DR HOGENOM; CLU_035788_0_0_2; -.
DR OrthoDB; 43786at2157; -.
DR Proteomes; UP000001903; 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:ADB62096.1};
KW Transferase {ECO:0000313|EMBL:ADB62096.1}.
FT DOMAIN 19..261
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 453 AA; 47571 MW; 2A47BB0FB6072C86 CRC64;
MRTPAPDSRP VALTIAGSDS GGGAGIQADL ATMAAHGVFG TSAITAVTAQ HTRGVESSHV
LPTAEIEAQI EAVTGDFAVG AAKTGMLATT PVIETVADYA REFEFPLLVD PVMVATSGDR
LLEAEAERAY EDLLGEATLA TPNADEAEVL TDIEVTDGES AVAAGEAILE TGVDAVLVKG
GHVPGETVRD TLVTEDGVRT FEHPRVGTEA THGSGCTLGS AIAARLATGE PLETAVEGAT
EFLARAVRYY YDVGEGHGAV NHMVSLRNEA SRELTAEEVQ AVVDRFVDAD VSALVPEVGM
NVAGATPYAE SVAETAAVEG RITRTLSGAQ PNRGVRFGAS SHVARFLLAA REFFPDLRFA
VNCRFDDDVE DALETLEWSV AEYDRDEQPD EVAETDGSTM GWGARQAFVD RDESPVAVVD
RGEIGKEAMV KLVASDPETL AERALALNGE VER
//
