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
//