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Database: UniProt
Entry: A0A099D6E1_9ACTN
LinkDB: A0A099D6E1_9ACTN
Original site: A0A099D6E1_9ACTN 
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
//
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