ID A0A099D6E1_9ACTN Unreviewed; 398 AA.
AC A0A099D6E1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Thiamine pyrophosphokinase {ECO:0000313|EMBL:ASU78554.1};
GN ORFNames=CDG81_09985 {ECO:0000313|EMBL:ASU78554.1};
OS Actinopolyspora erythraea.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU78554.1, ECO:0000313|Proteomes:UP000215043};
RN [1] {ECO:0000313|EMBL:ASU78554.1, ECO:0000313|Proteomes:UP000215043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU78554.1,
RC ECO:0000313|Proteomes:UP000215043};
RA Yin M., Tang S.;
RT "The complete genome sequence of moderately halophilic actinomycete
RT Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT novel actinopolysporins A-C and tubercidin.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP022752; ASU78554.1; -; Genomic_DNA.
DR RefSeq; WP_043572833.1; NZ_KN214176.1.
DR AlphaFoldDB; A0A099D6E1; -.
DR KEGG; aey:CDG81_09985; -.
DR eggNOG; COG4825; Bacteria.
DR HOGENOM; CLU_046690_0_0_11; -.
DR OrthoDB; 5169996at2; -.
DR Proteomes; UP000215043; 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:ASU78554.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 340..383
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
SQ SEQUENCE 398 AA; 42095 MW; 1EFC2D6D46252572 CRC64;
MRLSGLLGSR QEALPGLIGT ARVQRRIGEL PPRIGAREIV VLDEPDLDRR TAESLVAHEV
AAVVNAAPSI SGKYPNLGPE VLLAAGVVLV DDVGPEAPER IRDGATLRLY NGDVFLTGKR
GEEFLLHGSE QDAESVSARM AEAKSAMSAQ LEAFSANTIE FLRNERMLVL DGIGVPDVGV
AMAGRHVLVV APGRGHAEEL RRLRRYIREY RPVLLGVGAA ADTLHEAGLS PDVIVGDPAA
LDVRTLKAAD EVVIPADTDG HAPGIERIQD LGIGAVTFPA SGNPEDLALL LADAHDATLV
ATVGMRATLD EFLDRARAGT NPSTFLTRLR LGGKVVHGSA VLELQRNRVP TLAVLLLVLS
VVLAMFAVVS TSGMFGSYLT VLGAFGDTVV EFCRGLIT
//