ID A0A0R2RS62_9PROT Unreviewed; 968 AA.
AC A0A0R2RS62;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 Name=sucA {ECO:0000313|EMBL:KRO65487.1};
GN ORFNames=ABS03_03350 {ECO:0000313|EMBL:KRO65487.1};
OS Pelagibacteraceae bacterium BACL5 MAG-120820-bin39.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=1655605 {ECO:0000313|EMBL:KRO65487.1, ECO:0000313|Proteomes:UP000051468};
RN [1] {ECO:0000313|EMBL:KRO65487.1, ECO:0000313|Proteomes:UP000051468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL5 MAG-120820-bin39 {ECO:0000313|EMBL:KRO65487.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO65487.1}.
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DR EMBL; LIBV01000001; KRO65487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2RS62; -.
DR Proteomes; UP000051468; 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 ECO:0000313|EMBL:KRO65487.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 613..806
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 968 AA; 110659 MW; 12B7AB9E70C70740 CRC64;
MSLNKNLEFE KTSFLNKSNS AFIEEMYVRY INKDPELPKS WKEYFDDLGE EIEVIANEIK
GPSWNPLKKI KIKDISEDTQ EPTNGHLEKN NGALLGSDEI IKSNSDSIRA VALIRAYRQR
GHLLAKLDPL GMMKTEYLDE LHPEHYGFKS SDYKKEIYLD GVINKKKSNV REILDFLNKV
YCGPVGYEYM HITNPEERKW LRDRIELDKN ALEFTEIGKE GILNKLIQAE GFEKFLHTKY
VGTKRFGLDG GESLIPALEQ IIKIGGQSNV LEVKIGMSHR GRLNVLANVL QKSYKRIFNE
FTGDIHSPTK DGAGDVKYHL GASSDREFDG NSVHVSLTDN PSHLEAVNPV VLGQTRAKQY
FHKDKQRNKV IPILIHGDAA FAGQGIVAEC FAMSGLPGHN TGGTIHIIVN NQIGFTTSPR
FARSSPYPSD VAKMVEAPIF HVNGDDPEAV VYATRIATEF RLKFNRDVVI DLICYRRFGH
NEGDEPSFTQ PLMYKKIRSH PTVTNLYGKK LIEQKLFNEK SLKEKIDKFK DLLHDQFKNA
KDYKPKIEWF EGTWSRYKPE KGKDKRGISG VDEKVLKEIS NKINVIPADV SAHKTIIKIF
ESRKKSIDEG KNIDWATAEA LAFGSLVEQG FPVRLVGQDS GRGTFSQRHS VLRNQLNNKR
YVPLNNISKS QKQFEIVDSF LSELAVLGFE YGYSLVEPNT LTLWEAQFGD FANSAQVIID
QFISSGERKW SRASGLVMLL PHGYEGQGPE HSSARLERFL QLCSNDNMQV LNCTTPANYF
HALRRQMNRD FRKPLVIMTP KSLLRNKYCV SNLVDFNKKN SFHRVMWDHA IDPAYNGFIK
LKPSSKIRKV IMCSGKVYFD LLEAREKLKV DDVVLFRIEQ LYPFPAKSLV KEIKPYAKSA
KFYWCQEEPK NMGAWFSVRD YIQWTLDNIK ANNKEISYIG RSPDASPATG YAKRHISQQQ
EIIKKVFE
//
