ID A0A101G7S1_9FIRM Unreviewed; 373 AA.
AC A0A101G7S1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Thiamin pyrophosphokinase catalytic domain-containing protein {ECO:0000313|EMBL:KUK53339.1};
GN ORFNames=XD78_1283 {ECO:0000313|EMBL:KUK53339.1};
OS Desulfotomaculum sp. 46_296.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1635262 {ECO:0000313|EMBL:KUK53339.1, ECO:0000313|Proteomes:UP000053813};
RN [1] {ECO:0000313|Proteomes:UP000053813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK53339.1}.
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DR EMBL; LGFZ01000035; KUK53339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101G7S1; -.
DR STRING; 1635262.XD78_1283; -.
DR PATRIC; fig|1635262.3.peg.2120; -.
DR Proteomes; UP000053813; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR InterPro; IPR047795; Put_SteA-like.
DR InterPro; IPR022215; SteA-like_C.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR NCBIfam; NF040608; division_SteA; 1.
DR Pfam; PF12555; SteA-like_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, ECO:0000313|EMBL:KUK53339.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..227
FT /note="Thiamin pyrophosphokinase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04263"
FT DOMAIN 320..371
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
SQ SEQUENCE 373 AA; 40717 MW; 8D1B74221E8E598B CRC64;
MYIKGTARVD RRTKDLVKRL MPGEIAIINH SDLDNLAAQS LVAARPKAVI NAASSITGYY
PNPGPLLLVQ SGILLLDAAG EKIMGLVEEG RIIEIIDNEV YADGKCVGSG KFLEIQDIRD
KMAQANLNMN KVFCNFVENT IEHARNELGM VAGEYNIPTL STVLKGKHVL VVVRGQNYKE
DLETVRSYIH EVKPVLVGVD GGADALWEFG YKPDLIIGDM DSVSNDALFS GAELIVHAYP
DGRAPGLERI KNLGLPARTF AIPGTSEDIA MLLAYEQKAE LIVAVGTHSS VEDFLEKGRH
GMASTLLVRM KIGSILVDAK GVSKLYRGRI KARYLAQIVL AALLPLGVIV FISPVTRELL
RLVYLQFKLL LGI
//
