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Database: UniProt
Entry: T1C9N5_9ZZZZ
LinkDB: T1C9N5_9ZZZZ
Original site: T1C9N5_9ZZZZ 
ID   T1C9N5_9ZZZZ            Unreviewed;       492 AA.
AC   T1C9N5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:EQD62184.1};
GN   ORFNames=B2A_02952 {ECO:0000313|EMBL:EQD62184.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD62184.1};
RN   [1] {ECO:0000313|EMBL:EQD62184.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD62184.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQD62184.1}.
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DR   EMBL; AUZZ01001991; EQD62184.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1C9N5; -.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          208..400
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   492 AA;  55330 MW;  55FD9A248A56A5AC CRC64;
     MHVVINNQIG FTISRQDDAR STHYCTDIIK MINAPVLHVN GDDPEAVVFC ARLAFDYRQT
     FKRDIMIDLI CYRRHGHNEA DEPAATQPRM YQVIRGLPTT REQYAKRLAD AGTISAADAE
     QRAADYRRRL EAGESVTELS APLADAFRVD WSPYLNGTLG TEVATGVARD KLARLEAMLT
     DTTQIRLHPR VAKIYDDRRK MAAGQRPLDW GYAENLAYAT LLDAGYGLRL VGQDSARGTF
     FHRHAVLHDQ DTGATTLPLK RVREDAHVEI IDSALSEEAV MAYEYGFASA EPRTLPIWEG
     QFGDFANGAQ VVIDQFISSG EAKWDRLSAL TLFLPHGYEG QGPEHSSARL ERYLQLCALH
     NMQVCVPTTP AQVFHMIRRQ MLGQARKPLI VMTPKSLLRH KLAISSIDDL VRGGFQLVLP
     DTTAKTGQKV RRVVLCAGKV YYDLLEHAEK PASRMWRWCA SSSCTRSRAP PWRMNWNASR
     PPARWSGARR SP
//
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