ID I3YFC9_THIV6 Unreviewed; 942 AA.
AC I3YFC9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN OrderedLocusNames=Thivi_3855 {ECO:0000313|EMBL:AFL75697.1};
OS Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS violascens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocystis.
OX NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL75697.1, ECO:0000313|Proteomes:UP000006062};
RN [1] {ECO:0000313|EMBL:AFL75697.1, ECO:0000313|Proteomes:UP000006062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17096 / DSM 198 / 6111
RC {ECO:0000313|Proteomes:UP000006062};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of Thiocystis violascens DSM 198.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP003154; AFL75697.1; -; Genomic_DNA.
DR AlphaFoldDB; I3YFC9; -.
DR STRING; 765911.Thivi_3855; -.
DR KEGG; tvi:Thivi_3855; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR Proteomes; UP000006062; Chromosome.
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 CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 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 ECO:0000313|EMBL:AFL75697.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006062};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 588..781
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 942 AA; 105747 MW; 908542127357A91A CRC64;
MYGGNADFIE DLYERYLADP ESIDLAWRVR FDDMCQPAAN EAAETPHGPV RENFMRLAQE
SRSRARARST EHLEPAAAEK QSAVLGLITG YRYRGHQVAN LDPIHLRETP RIADLDPAYH
NLEPNDLDLV FHTGSLYAPD RMPLREIVAM VEQTYCGTVG SEYMHITSTP ERRWIQKRLE
GYRATPELDD ADRRWLLTLL TAAEGFEKYL HQRYVGQKRF SLEGGDALIP MLDELIQRAG
RKGQQEIVIG MAHRGRLNVL TNLFGKPPTD IFDEFEGRVH MDWRKMAGDV KYHMGFATDI
ETPGGIVHLV LGFNPSHLEI INPVIEGSVR ARQRRRLDRA GNLVLPVLIH GDAAFAGQGV
VMETLQLSQT RSYSTGGTVH IVINNQIGFT TSHPLDARSS AYCTDVGKLV QAPVFHVNGD
DPEAVIFVTR MALDFRNQFH KDVIIDLVCY RRLGHNEADE PAVTQPMMYA KIRNHPTPRA
VYADRLVAGG VIEKDAVDAM IADYRDSLEQ GVVVARPVLC GLDHLYRVDW GFCRGTDWDQ
DLDTGVPLAK LQALTEAMLR LPEGFALHPR VEKLWDERRK MGQGDQLLNW GFAENLAYAT
LLDAGIPVRL SGQDVGRGTF VHRHAKIHDQ LTGDSYTPLQ HLSDTQGAFI AIDSILSEEA
VLGYEYGFAT AEPTALTLWE AQFGDFANGA QVVIDQFITS AGTKWGLCCG LVMLLPHGLE
GQGAEHSSAR IERFLQLSAE HNIQVCVPTT PAQMFHLLRR QMVRDYRKPL IVMTPKSLLR
HRLAVSSLDE LAGGQFQTII PEIDPIDPAG VERLIFCCGK VYFDLLEARR ARSLTNAAII
RLEQLYPFPS EPFAAAIDHY GATEEIVWCQ EEPQNQGAWD QIKHRFHNLI QMGKRPYYVG
RASSAAPAVG HRAAHVEQHE RLIDEALTGQ FNPKMNKRIP PQ
//
