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Database: UniProt
Entry: A0A076MVK8_AMYME
LinkDB: A0A076MVK8_AMYME
Original site: A0A076MVK8_AMYME 
ID   A0A076MVK8_AMYME        Unreviewed;       412 AA.
AC   A0A076MVK8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Thiamin pyrophosphokinase catalytic region {ECO:0000313|EMBL:AIJ22785.1};
GN   ORFNames=AMETH_2693 {ECO:0000313|EMBL:AIJ22785.1};
OS   Amycolatopsis methanolica 239.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX   NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ22785.1, ECO:0000313|Proteomes:UP000062973};
RN   [1] {ECO:0000313|EMBL:AIJ22785.1, ECO:0000313|Proteomes:UP000062973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=239 {ECO:0000313|EMBL:AIJ22785.1,
RC   ECO:0000313|Proteomes:UP000062973};
RA   Tang B.;
RT   "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP009110; AIJ22785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A076MVK8; -.
DR   STRING; 1068978.AMETH_2693; -.
DR   KEGG; amq:AMETH_2693; -.
DR   PATRIC; fig|1068978.7.peg.2880; -.
DR   eggNOG; COG4825; Bacteria.
DR   HOGENOM; CLU_046690_0_0_11; -.
DR   Proteomes; UP000062973; 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:AIJ22785.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062973};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        363..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          353..404
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
SQ   SEQUENCE   412 AA;  43736 MW;  3C202ED1F000778C CRC64;
     MHGVLRADIR LSFATIGRMK LPGLLNRNTE ALPGIVGVAR VDRRTRDLLR RVGPGDIVVL
     DQIDLDRATA DALVEAEVAG VVNASPSISG RFPNLGPEIL VNAGIPLLDN VGGEVLRRIK
     DGSRIRLHEG GVYVGDRHVA SGSEQTPDSV ADQMIEAKAG MSTQLEAFSA NTIEFLRRER
     TLILDGVGVP EVRVPLRDRH VLVVAPGKGH AEDLKALRKY IAEHRPVLIG VDGGADTLRA
     QKYQPDIIVG DPFGIDAETL KCGAEVVVPA QPDGHAPGVA RIQDLGIGAV TFPASGNPED
     LALLLADAHE AGLVVTVGFQ ATLREFLDHG RSGSNPSTFL TRLKLGTRLV DGKAVAALHR
     SRVSLGAVVL LVVAALVAVA VALLMSDVGG AYLDWARSTW DSFTSWVKGL FT
//
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