ID A0A147IQ31_9SPHN Unreviewed; 992 AA.
AC A0A147IQ31;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:KTT97258.1};
GN ORFNames=NS355_12050 {ECO:0000313|EMBL:KTT97258.1};
OS Sphingomonas yabuuchiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=172044 {ECO:0000313|EMBL:KTT97258.1, ECO:0000313|Proteomes:UP000073923};
RN [1] {ECO:0000313|EMBL:KTT97258.1, ECO:0000313|Proteomes:UP000073923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS355 {ECO:0000313|EMBL:KTT97258.1,
RC ECO:0000313|Proteomes:UP000073923};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTT97258.1}.
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DR EMBL; LDTF01000064; KTT97258.1; -; Genomic_DNA.
DR RefSeq; WP_058745939.1; NZ_LDTF01000064.1.
DR AlphaFoldDB; A0A147IQ31; -.
DR PATRIC; fig|172044.3.peg.2412; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000073923; 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:KTT97258.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 622..813
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 53..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 109036 MW; DCD52B7C951B1936 CRC64;
MGYEGQEFSD IAAGVSPAFI ETLYAKYQAD QSSVDAGWRT FFEGLEQGVG APSWQNKRWP
LTSTDDLTAG LDPTQMEPAP KPAKGGKPAA APAAAAPSTA DIVKAAGDAI RAQLLIRTYR
VRGHLAANLD PLGLSGLREL PEDLKTEYHG FTDADIDRKV YLGGTMGFEW ATVRELVDTL
RKNYCGNIGL EYMHIADVEE RRFLQDRMEG QDKAIDFTVD GKKAILNKVI EAEQWEKFLG
KKYVGTKRFG LDGGESMIPA LESVIKYGGQ MGVREIVFGM AHRGRLNVLA NVMAKPLRVI
FHEFAGGSAN PDDIGGSGDV KYHLGTSTDR EFDGHKVHMS LVANPSHLEA VNPVVLGKTR
AIQTIAGDLE DHSASVPVLI HGDAAFAGQG IVWECLGFSG IRGYNTGGCV HFIINNQVGF
TTSPQFARSS PYPSDVAKGV QAPVFHVNGD DPEAVTFATK MAIEFRQKFH RDIVIDMWCY
RRFGHNEGDE PGFTQPLMYN KIRSHPGVAE TYAKRLVSEG VVDQAWVDEN IKQYTTRCEG
EFEAGASYKP NKADWFAGRW SGLSAPKETD QGRRNVETGL DKKLFDAIGR TLTTIPEGLQ
VHKTLNRVLD AKRQMFATGE NFDWATGEAL AFGSLLSEGY GVRLSGQDSG RGTFSQRHAV
WVDQTDEHKY VPLKTVEHGS FEVLDSPLSE YGVLGFEYGY ALADPKTLVM WEAQFGDFVN
GAQIMIDQFI TSGESKWLRA NGLVMLLPHG YEGQGPEHSS ARPERFLQSC ANDNIQVANC
TTPANYFHLL RRQMHRNFRK PLIVMTPKSL LRHKLAVSKA EDFQGESHFR RLLSDTNGAA
DEATTRLVLC TGKVAYDLIE ARDAAGDTGT QIVRVEQLYP FPSDALAKRI ARMPNLQDVV
WAQEEPKNNG YWFFVEPLIE ESLAAAGASV KRARYAGRAA AASPATGLMK RHTAEQGALV
ADALGHNVRE EIRRTRAEGS NTTAKPTTAA AD
//
