ID A0A0K1RAI6_9CORY Unreviewed; 389 AA.
AC A0A0K1RAI6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Thiamine pyrophosphokinase {ECO:0000313|EMBL:AKV58440.1};
GN ORFNames=AK829_03795 {ECO:0000313|EMBL:AKV58440.1};
OS Corynebacterium riegelii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156976 {ECO:0000313|EMBL:AKV58440.1, ECO:0000313|Proteomes:UP000060016};
RN [1] {ECO:0000313|EMBL:AKV58440.1, ECO:0000313|Proteomes:UP000060016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PUDD_83A45 {ECO:0000313|EMBL:AKV58440.1,
RC ECO:0000313|Proteomes:UP000060016};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012342; AKV58440.1; -; Genomic_DNA.
DR RefSeq; WP_052204414.1; NZ_CP012342.1.
DR AlphaFoldDB; A0A0K1RAI6; -.
DR STRING; 156976.AK829_03795; -.
DR PATRIC; fig|156976.3.peg.748; -.
DR Proteomes; UP000060016; 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 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:AKV58440.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000060016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 342..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 329..381
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
SQ SEQUENCE 389 AA; 41032 MW; 9AB1972427207A35 CRC64;
MTVSTSINGT LRDCTAQGKG IGRLSEGDIA FVDAPDMTRR FAELLVAAKP AAVVNVARFT
TGLIPNYGPH VLLDAGIPLY EAAGSSMRGV VKDGKKASVS PTGEVMMGKK LIGQASAVSR
EDVDATFADA QQALVDNMEA YFGNTIQFIH SEAPLLIDGV GSPELGDTMA ERKVLVVSQS
EDLRERLDGL KFFIREYTPV IIGVGAAADT LTKLGYDMDF IVGDPTDISN EALRGDAKVI
LPAETDGFAP GLERIQDLGV GAMTFPAATD SPTDLAILLA VFHDAEMVIT VGQPVELDSI
FADAAAAEPA ALLTRLKAGR KLVDSTVIEH LYDTNTGGGG VAWAWAILGL LVAAATVVLI
VGLGGSETFT TNLVDTWNRI ALEFQSWFN
//
