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Database: UniProt
Entry: Q8NTY9_CORGL
LinkDB: Q8NTY9_CORGL
Original site: Q8NTY9_CORGL 
ID   Q8NTY9_CORGL            Unreviewed;       576 AA.
AC   Q8NTY9;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   28-FEB-2018, entry version 77.
DE   SubName: Full=Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (Cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase] {ECO:0000313|EMBL:BAB97555.1};
GN   OrderedLocusNames=Cgl0162 {ECO:0000313|EMBL:BAB97555.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
OS   LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB97555.1, ECO:0000313|Proteomes:UP000000582};
RN   [1] {ECO:0000313|Proteomes:UP000000582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
RC   {ECO:0000313|Proteomes:UP000000582};
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; BA000036; BAB97555.1; -; Genomic_DNA.
DR   RefSeq; NP_599414.1; NC_003450.3.
DR   ProteinModelPortal; Q8NTY9; -.
DR   STRING; 196627.cg0202; -.
DR   EnsemblBacteria; BAB97555; BAB97555; BAB97555.
DR   GeneID; 1021162; -.
DR   KEGG; cgl:NCgl0159; -.
DR   PATRIC; fig|196627.13.peg.166; -.
DR   eggNOG; ENOG4107QK6; Bacteria.
DR   eggNOG; COG3962; LUCA.
DR   KO; K03336; -.
DR   OMA; LPKTMTH; -.
DR   BioCyc; CORYNE:G18NG-9711-MONOMER; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_iolD.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968:SF9; PTHR18968:SF9; 2.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR04377; myo_inos_iolD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000582};
KW   Ligase {ECO:0000313|EMBL:BAB97555.1};
KW   Pyruvate {ECO:0000313|EMBL:BAB97555.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000582};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        1    141       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      164    298       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      361    529       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   576 AA;  61894 MW;  3AAE25029ED6BD55 CRC64;
     MPYYQARNEQ AMVHQSVGYA RMHRRRGTYA SAASVGPGAT NLLTGAALAT TNRLPALLLP
     SDTFATRVAD PVLQQLEQPW DIGLTVNDAF RPVSKFFDRV QRPEQLFSIA LAAMRVLTDP
     AETGAVTIAL PEDVQAEMLD VPVEFLQDRE WHIRRPRPER AALARAIEVI KNAKNPMIIA
     GGGVLYSDAE TQLQALVEQT GIPVGTSQAG GGVLAWDHAQ NLGGVGATGT LAANRIAGDA
     DVIIGIGTRY SDFTTASRTA FQNPDVTFIN INVASFDAYK HGTQLPVIAD AREAIVELAE
     ALQGFTVAED YAQRIAKEKA AWDAEVDKSF APSGLALPGQ PEIIGAVQAS TSEKDVIVQA
     AGSLPGDLHK LWRVRDALGY HVEYAFSCMG YEIAGGIGAK RGLDAAGDDR DVVIMVGDGS
     YLMLNTELVT AVAEGIKVIV VLIQNHGYAS IGHLSETVGS QRFGTWYREY DAEAKNFQGE
     QILPVDLAMN ARSYGMDVIE VEPSANAIED LKAAMATAKA SEKSTFIHIN SDPLIYAPDG
     AGWWDVPVSE TSTLDSTNAA REDYLKNQAL QRPLLG
//
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