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Database: UniProt
Entry: A0A1D8T4Y5_9NOCA
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ID   A0A1D8T4Y5_9NOCA        Unreviewed;       394 AA.
AC   A0A1D8T4Y5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Thiamine pyrophosphokinase {ECO:0000313|EMBL:AOW92751.1};
GN   ORFNames=BFN03_08755 {ECO:0000313|EMBL:AOW92751.1};
OS   Rhodococcus sp. WMMA185.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW92751.1, ECO:0000313|Proteomes:UP000178767};
RN   [1] {ECO:0000313|EMBL:AOW92751.1, ECO:0000313|Proteomes:UP000178767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMMA185 {ECO:0000313|EMBL:AOW92751.1,
RC   ECO:0000313|Proteomes:UP000178767};
RA   Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT   "Draft Genome of Rhodococcus sp. WMMA185.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP017014; AOW92751.1; -; Genomic_DNA.
DR   RefSeq; WP_070378690.1; NZ_CP017014.1.
DR   AlphaFoldDB; A0A1D8T4Y5; -.
DR   STRING; 679318.BFN03_08755; -.
DR   KEGG; rhw:BFN03_08755; -.
DR   OrthoDB; 5169996at2; -.
DR   Proteomes; UP000178767; Chromosome.
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; 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:AOW92751.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000178767};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        349..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          335..386
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   394 AA;  41631 MW;  016D017BC0110D36 CRC64;
     MKLPALRSRN TQPLPGVSGI ARVDRNTDKL LRRVGPGDVV VLDELDLDRR TADALVKAGV
     LAVINASPSI SGRYPNLGPE VIVSNGIALV DSVGTEVFKN IKDGGKVRVH EGAVYSGERR
     IAKGDAQTEA EISDRMIEAK TGLVDHLEAF SGNTIEFIRT ESPLLIDSVG VPDVDVDMKE
     RHVVIVSDGP DHVSDLKNLK PFIKEYSPIL IGVGTGADAL KTAGYRPDLI VGDPEAISSA
     TLKSGAEVVL PADQDGHAPG LSRIQDLGIG AMTFPASGSP SDLALLLADH HGAALIVTVG
     STVSLDEFFD RGRRDINPSA FMTRLKVGPK LVDAKAVATL YRSRVSGGAI ALLILAALVA
     VIVALAMSNV GGEVLDWAVA TWDSFVLWVQ GFFK
//
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