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Entry: G1VHT3_9BACT
LinkDB: G1VHT3_9BACT
Original site: G1VHT3_9BACT 
ID   G1VHT3_9BACT            Unreviewed;       317 AA.
AC   G1VHT3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=HTH araC/xylS-type domain-containing protein {ECO:0000259|PROSITE:PS01124};
GN   ORFNames=HMPREF0666_02966 {ECO:0000313|EMBL:EGW49269.1};
OS   Prevotella sp. C561.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=563031 {ECO:0000313|EMBL:EGW49269.1, ECO:0000313|Proteomes:UP000003086};
RN   [1] {ECO:0000313|EMBL:EGW49269.1, ECO:0000313|Proteomes:UP000003086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C561 {ECO:0000313|EMBL:EGW49269.1,
RC   ECO:0000313|Proteomes:UP000003086};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA   Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. C561.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC         amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC         Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC         methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC         Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC         EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGW49269.1}.
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DR   EMBL; ADCT01000113; EGW49269.1; -; Genomic_DNA.
DR   RefSeq; WP_009013029.1; NZ_JH114155.1.
DR   AlphaFoldDB; G1VHT3; -.
DR   STRING; 563031.HMPREF0666_02966; -.
DR   PATRIC; fig|563031.3.peg.2832; -.
DR   eggNOG; COG0351; Bacteria.
DR   eggNOG; COG2207; Bacteria.
DR   HOGENOM; CLU_020520_0_0_10; -.
DR   Proteomes; UP000003086; Unassembled WGS sequence.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
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; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   PRINTS; PR00032; HTHARAC.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125}.
FT   DOMAIN          219..317
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
SQ   SEQUENCE   317 AA;  35247 MW;  5AC9F8E7B4F6B7FE CRC64;
     MKTILTITGS DSTGGSGVQA DIRTIAALGG YAVSAVTSVT VQNTLGIQAF YDLPAEIVRG
     QIEAIINDMQ PDTVKVGMIR TTETLAVVVD VLLKYRPHHI IYDPIVTASN GDRLLSDDVI
     TQIRCRLLPL CSLVILREGE TEKIFSSPSL KGKKETDVCT YVLDDPLQHG LANSFSSSLA
     VYLSQDEPME QAIKHAREYV RTLITRKSDI SGRSSQLYYE FLEAVQLHYR TNRDVAFYAD
     CLNVSPRYLS QVAHRISGKS PKTIIDHTLA DALACQLRTT QKTIQEIAYE HGFASQAQFS
     KFFKKLMGHS PSEWRRT
//
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