ID A0A0I9UL37_9MYCO Unreviewed; 393 AA.
AC A0A0I9UL37;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Thiamine pyrophosphokinase {ECO:0000313|EMBL:KLO37207.1};
GN ORFNames=ABH38_09965 {ECO:0000313|EMBL:KLO37207.1};
OS Mycobacterium haemophilum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO37207.1, ECO:0000313|Proteomes:UP000036334};
RN [1] {ECO:0000313|EMBL:KLO37207.1, ECO:0000313|Proteomes:UP000036334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium haemophilum.";
RL Submitted (MAY-2015) 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:KLO37207.1}.
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DR EMBL; LDPR01000006; KLO37207.1; -; Genomic_DNA.
DR RefSeq; WP_047313993.1; NZ_LDPT01000003.1.
DR AlphaFoldDB; A0A0I9UL37; -.
DR STRING; 1202450.B586_12330; -.
DR PATRIC; fig|29311.18.peg.2812; -.
DR OrthoDB; 5169996at2; -.
DR Proteomes; UP000036334; 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 InterPro; IPR047795; Put_SteA-like.
DR InterPro; IPR022215; SteA-like_C.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR NCBIfam; NF040608; division_SteA; 1.
DR Pfam; PF12555; SteA-like_C; 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:KLO37207.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000036334};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..384
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
SQ SEQUENCE 393 AA; 42341 MW; DA3FD3C7941DD739 CRC64;
MRMSALLSRN TSRPGLVGTA RVDRNIDRLL RRVCPGDIVV LDVLDLDRIT ADALVEADIA
AVVNASPSVS GRYPNLGPEV LVNNGVTLID ETGPEVFKKI KDGAKIRLHE GGVYAGDRRL
IRGTERTDHD IADLMREAKS GLAAHLEAFA GNTIEFIKSE SPLLIDGIGI PDIDVDLRRR
HVVIVADEPS AADDLKSLKP FIKEYQPVLV GVSGGADVLR KAGYRPQLIV GDPEQISTEA
LKCGAHVVLP ADADGHAPGL ERIQDLGVGA MTFPAAGSAT DLALLLADHH GAALLVTAGH
TANIETFFDR TRTQSNPSTF LTRLRVGEKL VDAKAVATLY RNHISAGAIA LLAMTMLIAV
IVALWVSRTD GVVLHWVVDY WNRFSLWIQH LVA
//
