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Database: UniProt
Entry: R6L8C0_9BACE
LinkDB: R6L8C0_9BACE
Original site: R6L8C0_9BACE 
ID   R6L8C0_9BACE            Unreviewed;       219 AA.
AC   R6L8C0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDB70492.1};
GN   ORFNames=BN506_01935 {ECO:0000313|EMBL:CDB70492.1};
OS   Bacteroides cellulosilyticus CAG:158.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1263038 {ECO:0000313|EMBL:CDB70492.1, ECO:0000313|Proteomes:UP000018191};
RN   [1] {ECO:0000313|EMBL:CDB70492.1, ECO:0000313|Proteomes:UP000018191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:158 {ECO:0000313|Proteomes:UP000018191};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDB70492.1}.
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DR   EMBL; CBEB010000096; CDB70492.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6L8C0; -.
DR   Proteomes; UP000018191; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR   CDD; cd07995; TPK; 1.
DR   Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR   InterPro; IPR006282; Thi_PPkinase.
DR   InterPro; IPR049442; Thi_PPkinase-like_C.
DR   InterPro; IPR007371; TPK_catalytic.
DR   InterPro; IPR036759; TPK_catalytic_sf.
DR   NCBIfam; TIGR01378; thi_PPkinase; 1.
DR   PANTHER; PTHR41299; THIAMINE PYROPHOSPHOKINASE; 1.
DR   PANTHER; PTHR41299:SF1; THIAMINE PYROPHOSPHOKINASE; 1.
DR   Pfam; PF21275; Thi_PPkinase_C; 1.
DR   Pfam; PF04263; TPK_catalytic; 1.
DR   SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018191};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          38..141
FT                   /note="Thiamin pyrophosphokinase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF04263"
FT   DOMAIN          148..215
FT                   /note="Thiamin pyrophosphokinase-like substrate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21275"
SQ   SEQUENCE   219 AA;  24214 MW;  7D3FE406671BBF31 CRC64;
     MMKENNNKNS VELCVLCGEP EAVILANGDY PTHPIPLQIL ANAPYIICCD GGADAYIDRG
     NVPDVIIGDG DSLSKENRRK YSHILHCVSD QETNDQTKAV NFLLSQGKKN IAIVGATGKR
     EDHTLGNISL LIDYMRTGAH VRMLTDYGIF IPCHDTCSFP SQPGQQISII NFGAHNLRGK
     GLVYPLSDFT NWWQGTLNES TETEFTIHAK GEYLVVINY
//
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