ID Q2RV31_RHORT Unreviewed; 983 AA.
AC Q2RV31;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 OrderedLocusNames=Rru_A1213 {ECO:0000313|EMBL:ABC22014.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22014.1, ECO:0000313|Proteomes:UP000001929};
RN [1] {ECO:0000313|EMBL:ABC22014.1, ECO:0000313|Proteomes:UP000001929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC {ECO:0000313|Proteomes:UP000001929};
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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}.
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DR EMBL; CP000230; ABC22014.1; -; Genomic_DNA.
DR RefSeq; YP_426301.2; NC_007643.1.
DR AlphaFoldDB; Q2RV31; -.
DR STRING; 269796.Rru_A1213; -.
DR EnsemblBacteria; ABC22014; ABC22014; Rru_A1213.
DR KEGG; rru:Rru_A1213; -.
DR PATRIC; fig|269796.9.peg.1278; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR PhylomeDB; Q2RV31; -.
DR Proteomes; UP000001929; 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:ABC22014.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001929};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 618..811
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 983 AA; 109304 MW; F933B13CC9BF575C CRC64;
METSFLTGAN AVYIAEVYSR YLADPSSVDP SWVAFFGELR DGAEELSGDL KGPSWTSRGN
AVIGTADPDA PAAAKAGKNG KAAAAPVPAA PAAAGLSTAE VRAHTLDSVR ALMMIRAYRV
RGHLVADLDP LGLNKNNEHP ELDYRSYGFT DADLEREIFI DNVLGMESAT LRKIVEVVRE
TYCGTIGVEF MHIQDPEQKS WIQRRIEGER NHTRFTPEGK RAILERLTEA EGFEKFLQVK
YTGTKRFGLE GGETVIPAIE QILKRGSQLG LTDINLGMAH RGRLNLLTSL LHKPYRAIFS
EFQGNSANPD DVQGSGDVKY HLGTSADREF DGAVVHLSLQ ANPSHLEAAD PVVLGKVRAK
QTQLGDTDRK AVMALLIHGD AAFAGQGLVA ECFGLSQLKG YRTGGTIHIV INNQIGFTTS
PQYSRSGQYC TDIAKMVQAP IFHVNGDDPE AVVHTARIVT EFRQEFGVDV VLDMVCYRRH
GHNESDEPAF TQPLMYDSIA HRQTTRTLYA QKLVSEGLIS QAEADGLADA FTARLETEFQ
AATSYKPNRA DWLAGKWEGL EALNGEEEFR QDRTEVPAEV LRRVGTALST PPENFDTNRK
ILRQMKAKAE MLETGQGIDW ATAEALAFGT LLLEGTRVRL SGQDSGRGTF SHRHSVLIDQ
TNENRHIPLD HLDPAQARFE VIDSPLSEFS VLGFEYGYSL AEPKALVLWE AQFGDFANGA
QVIFDQFISS AESKWLRMSG LVCLLPHGYE GQGPEHSSAR PERYLQLCAE DNMQVVNITS
PANYFHALRR QVHRNFRKPL IVMAPKSLLR HKLAVSPLSD FTDHGFRRVL PETKTLVEDD
KITRVVLCSG KVYYDLYQAR EDQGIDDVAI VRIEQLYPWP KDTLMKVLKR YPNADVVWCQ
EEPANMGYWT FVDRRIEFFL QELEHRPGRA SYAGRPAAAS PATGSNRGHG REQALLVEQA
LTWKRDVLPQ PFRRATKLSI IGQ
//
