ID H6RWF1_BLASD Unreviewed; 395 AA.
AC H6RWF1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Thiamin pyrophosphokinase {ECO:0000313|EMBL:CCG03366.1};
GN OrderedLocusNames=BLASA_2485 {ECO:0000313|EMBL:CCG03366.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG03366.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG03366.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG03366.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FO117623; CCG03366.1; -; Genomic_DNA.
DR RefSeq; WP_014376249.1; NC_016943.1.
DR AlphaFoldDB; H6RWF1; -.
DR STRING; 1146883.BLASA_2485; -.
DR KEGG; bsd:BLASA_2485; -.
DR eggNOG; COG4825; Bacteria.
DR HOGENOM; CLU_046690_0_0_11; -.
DR OrthoDB; 5169996at2; -.
DR Proteomes; UP000007517; 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; 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:CCG03366.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007517};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 350..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 210..300
FT /note="Thiamin pyrophosphokinase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04263"
FT DOMAIN 336..387
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 41872 MW; D1211C5A68630350 CRC64;
MRIGTVRRGR AQDTGPGVAG TVRLDRRTKN LTKRLRPGDI AVIDHVDIDR VSADALVGCR
VAGVVNAAPS ISGRYPNLGP GILLDAGIPL LDDVGRDVFA KIKEGAEVRL DGNRLLDEQG
TVVAEGTAHD AETVAAAMAD AKAGLSVQLE AFAANTMEYM KRERALLLDG VGVPDVATSI
EGRHVLVVVR GYDYKEDLHA LRSYIRDYRP VLIGVDGGAD ALVDAGYSPD MIIGDMDSVS
DDVLRCGAEV VVHAYADGRA PGLARVQDLG VEAITFPAAA TSEDIAMLLA DEKGATLIVA
VGTHATLVEF LDKGRGGMAS TFLTRLRLGG KLVDAKGVSR LYRSRISTTV LVIMVLAALL
AIGAALAVSA VGRVYVDLLL DQWNSFVFWL ENLFS
//
