ID K8EBC4_9FIRM Unreviewed; 373 AA.
AC K8EBC4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Thiamin pyrophosphokinase, catalytic region {ECO:0000313|EMBL:CCO08938.1};
GN ORFNames=DESHY_60110 {ECO:0000313|EMBL:CCO08938.1};
OS Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO08938.1, ECO:0000313|Proteomes:UP000009315};
RN [1] {ECO:0000313|EMBL:CCO08938.1, ECO:0000313|Proteomes:UP000009315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT hydrothermale Lam5(T).";
RL Genome Announc. 1:e00114-e00112(2013).
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:CCO08938.1}.
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DR EMBL; CAOS01000013; CCO08938.1; -; Genomic_DNA.
DR RefSeq; WP_008412637.1; NZ_FQXF01000004.1.
DR AlphaFoldDB; K8EBC4; -.
DR STRING; 1121428.DESHY_60110; -.
DR eggNOG; COG4825; Bacteria.
DR OrthoDB; 9804377at2; -.
DR Proteomes; UP000009315; 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:CCO08938.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 334..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..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; 40950 MW; F3121EE19B4E4CD7 CRC64;
MNIKAIARID KRTKDLAKRI NANEIAVICH YELDKVAADS LLAAKVKAVI NAVPSMSEDY
PNQGPITLLE AGIPILDNVG KEIMEKIHEG EELEIRGNLV LRQGEVVAAG TRLTLQQVKE
HMEQSRSRMD RVLSRFIHNT LDYARNEVDF VCGGLQIPEI TTSFKGRHTL IVVRGHNYKQ
DLNAIKSYID EVRPVLIGVD GGADALLEFG YTPDLIIGDM DSTTDKALCS GAELVVHAYP
DGRAPGMERI KALGLQAKVF PAPGTSEDIA MMLAYEKGTE LIVAVGTHSN MLDFLEKGRK
GMASTFLVRL KVGDILVDAK GVSQLYRSRM KLKYVGQLLL AGLVPLAVVM AMAPPTRELL
RLLVLNVRLI FGI
//
