ID U4V889_9RHOB Unreviewed; 988 AA.
AC U4V889;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN ORFNames=HIMB11_00729 {ECO:0000313|EMBL:ERL98921.1};
OS Rhodobacteraceae bacterium HIMB11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL98921.1, ECO:0000313|Proteomes:UP000016848};
RN [1] {ECO:0000313|EMBL:ERL98921.1, ECO:0000313|Proteomes:UP000016848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB11 {ECO:0000313|EMBL:ERL98921.1,
RC ECO:0000313|Proteomes:UP000016848};
RA Durham B.P., DeLong E.F., Rappe M.S.;
RT "Draft genome sequence of marine alphaproteobacterial strain HIMB11, the
RT first cultivated representative of a unique lineage within the Roseobacter
RT clade possessing a remarkably small genome.";
RL Submitted (AUG-2013) 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:ERL98921.1}.
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DR EMBL; AVDB01000002; ERL98921.1; -; Genomic_DNA.
DR AlphaFoldDB; U4V889; -.
DR STRING; 1366046.HIMB11_00729; -.
DR PATRIC; fig|1366046.3.peg.733; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000016848; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000016848};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 632..825
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 988 AA; 110763 MW; EAD1A72AE525474A CRC64;
MTDQSNSAQF HASSFMQGHN AEYLEQLYAQ YAKDPNAVDA AWAEFFRAMG DDEVSVKAEA
EGPSWARTDW PQQPCDDWTN ALTGEWPVVA AEGKSAGKKI ADKAKEKDVE VSDEAMKRAV
LDSIRAIMLI RAYRVRGHLA ADLDPLNMRD TKDAEASLDP KNYGFTDADM DRPIFLDNVL
GLQIASMRQI IDIVRRTYCG TFALQYMHIS DPEQSAWLKE RIEGFGKEIT FTREGRKAIL
NKLVEAEGFE KFLHVKYMGT KRFGLDGGEA LIPALEQIIK RGGALGVKDV VIGMPHRGRL
SVLANVMNKP YRAIFNEFQG GSFKPEDVDG SGDVKYHLGA SSDREFDGNS VHLSLTANPS
HLEAVNPVVL GKVRAKQEQL NDEDRTQVMP LLLHGDAAFA GQGVVAECFG LSGLVGHKTG
GTMHVVVNNQ IGFTTAPHFS RSSPYPTDIA LMVEAPIFHV NGDDPEAVVH AAKVATEFRQ
KFQKDVVIDI FCYRRFGHNE GDEPMFTNPM MYKNIKQHKT TLALYTERLV RDGLIPEGEI
EDMKAAFQAK MNDEFEAGRD YKPNKADWLD GRWSHLDREK DDYQRGQTSI SDETLSTVGM
ALTTAPEGFA LHKTVARLLD TKSKMFESGK GFDWATAEAL AFGSLLTEGY PVRLAGQDAT
RGTFSQRHSG LINQNDESRY YPLNNIREGQ SRYDVIDSML SEYAVLGFEY GYSLSEPNAL
VMWEAQFGDF ANGAQIMFDQ FISSGESKWL RMSGLVVLLP HGFEGQGPEH SSARLERFLQ
MCGQDNWIVA NCSTPANYFH ILRRQIHRSF RKPLILMTPK SLLRHRLCIS EAADFTDGSS
FHRVLWDDAQ KGNSDTELVA DDKIKRVVMC SGKVYYDLLE ERDRRGIDDV YLLRFEQFYP
FPALAALKEL ERFKNAEMVW CQEEPKNQGA WSFMEPNLEW VLTRMNAKHP RPVYAGRAAS
ASPATGLAST HKAQQEALID DALTIKGN
//
