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Database: UniProt
Entry: A1UJ25_MYCSK
LinkDB: A1UJ25_MYCSK
Original site: A1UJ25_MYCSK 
ID   A1UJ25_MYCSK            Unreviewed;       368 AA.
AC   A1UJ25;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   SubName: Full=Thiamine pyrophosphate enzyme domain protein TPP-binding protein {ECO:0000313|EMBL:ABL92833.1};
GN   OrderedLocusNames=Mkms_3639 {ECO:0000313|EMBL:ABL92833.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92833.1};
RN   [1] {ECO:0000313|EMBL:ABL92833.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL92833.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000518; ABL92833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UJ25; -.
DR   STRING; 189918.Mkms_3639; -.
DR   KEGG; mkm:Mkms_3639; -.
DR   HOGENOM; CLU_048564_1_0_11; -.
DR   OMA; GNDTWTV; -.
DR   OrthoDB; 9775140at2; -.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03375; TPP_OGFOR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          83..230
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          23..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  40097 MW;  C0D2E383CA5D3B89 CRC64;
     MTTARSEADR ATQLIGTDLS LTPLSKTAGV PTTDQPQKGK DFTSDQEVRW CPGCGDYVIL
     NTIRNFLPEL GLRRENIAFI SGIGCSSRFP YYLETYGFHS IHGRAPTIAT GLALARPDLS
     VWVVTGDGDS LSIGGNHLIH ALRRNINITI LLFNNRIYGL TKGQYSPTSE VGKVTKSTPM
     GSLDYPFNPV SLALGSEATF VGRALDSDRK GLSEVLRAAA QHRGAALVEI LQDCPIFNDG
     SFDALRKEGA EERLINVRHG EPITFGADGE YCVVKSGYGL EVAKTADVPA EEIVVHNAQI
     DDPAYAFALS RLSEQNLDHM VMGIFRQVNR PTYDDAAREQ VSSAREAKPH DTAALQSLLR
     GKDTWTVD
//
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