ID   A0A2T4JL83_9RHOB        Unreviewed;       724 AA.
AC   A0A2T4JL83;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   ORFNames=C5F46_03440 {ECO:0000313|EMBL:PTE18665.1};
OS   Phaeovulum veldkampii DSM 11550.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Phaeovulum.
OX   NCBI_TaxID=1185920 {ECO:0000313|EMBL:PTE18665.1, ECO:0000313|Proteomes:UP000241899};
RN   [1] {ECO:0000313|EMBL:PTE18665.1, ECO:0000313|Proteomes:UP000241899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11550 {ECO:0000313|EMBL:PTE18665.1,
RC   ECO:0000313|Proteomes:UP000241899};
RA   Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA   Chintalapati V.R.;
RT   "Rhodobacter veldkampii.";
RL   Submitted (MAR-2018) 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};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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:PTE18665.1}.
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DR   EMBL; PZKF01000005; PTE18665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4JL83; -.
DR   OrthoDB; 7821727at2; -.
DR   Proteomes; UP000241899; Unassembled WGS sequence.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241899}.
FT   DOMAIN          394..575
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   724 AA;  78081 MW;  E0B9DFC8CB5BE422 CRC64;
     MPRSEIVHES FLRRVTARDF PSGKAPEPGL SAADAVRLYR AQCLSRALDR QSRAMQKAGQ
     GYYTIGSSGH EGMAAVAHAA RPTDMAFLHY RDAAFQIARA DQVPGQDMCR DMLLSFACAA
     EDPISGGRHK VLGSKALTIP PQTSTIASHL PKAVGAAFSL GLARRHPPEH RALAEDAIIL
     CSFGDASANH STAQGALNTA SWTAYQGLPL PLLFVCEDNG IGISTRTPNG WIKASQAARP
     GVRYFAADGL DLYQTFAVAA EAADYVRRCR KPAFLHLRMV RLYGHAGADL PTTYMAREEV
     EAEEANDPLL HSVRLLDLAG ALAPDQALAI YTETLDRVAQ VAAEVVTRPR LRTAAEVMES
     LIPPARPCAA RNGPGPEARA EAFGADLKAM DEPQPMSRLL NWALTDLMVT HPEIVLMGED
     VGRKGGVYGV TQKLFTRFGA GRVMDTLLDE QSILGLGIGM AHNGFLPVPE IQFLAYLHNA
     EDQLRGEAAT LPFFSRGQFS NPMVVRIAGL GYQKGFGGHF HNDNSLAVLR DIPGLILACP
     SRGAEAAMML RECVRLARED QRVVVFLEPI ALYPMRDLHR DKDGLWMDHY PAPDQRIGFG
     TVGTQGTGRD LAIITYGNGV YLSHQAEPAL RAAGIDLRIV DLRWLAPLPE AAIRAAAQDC
     AAVLVVDECR RSGNLSEALM TLLADHPCKA RLTAEDSFIA TGPAYAATLP SAQGIVTAAL
     ALLR
//