ID T0IE42_9SPHN Unreviewed; 949 AA.
AC T0IE42;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN Name=sucA {ECO:0000313|EMBL:EQB07919.1};
GN ORFNames=L284_22300 {ECO:0000313|EMBL:EQB07919.1};
OS Novosphingobium lindaniclasticum LE124.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB07919.1, ECO:0000313|Proteomes:UP000015527};
RN [1] {ECO:0000313|EMBL:EQB07919.1, ECO:0000313|Proteomes:UP000015527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LE124 {ECO:0000313|EMBL:EQB07919.1,
RC ECO:0000313|Proteomes:UP000015527};
RX PubMed=24029761;
RA Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT a Hexachlorocyclohexane Dumpsite.";
RL Genome Announc. 1:e00715-13(2013).
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:EQB07919.1}.
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DR EMBL; ATHL01000152; EQB07919.1; -; Genomic_DNA.
DR RefSeq; WP_021236125.1; NZ_ATHL01000152.1.
DR AlphaFoldDB; T0IE42; -.
DR PATRIC; fig|1096930.3.peg.4388; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000015527; 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; 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; 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:EQB07919.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015527};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 594..785
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 104936 MW; 2D99D308605D89B8 CRC64;
MGDESFDFTP DEALDGPQAG PSWQRKNWPL VGAEFEDDLT QGLDPSALKI KIEKAAAKGG
QKVDQSRIDE AAADAIRAMM LIRTYRVRGH LAADLDPLGL NQRNLPADLT PEYHGFVGAA
QDRPVYVGGA LGLEWTTVRE IVQILRANYC GKVGLEYMHI ADVEERRFLQ ERMEGADKEI
EFTPEGKKAI LQAVVRGEQY EKFLGKKYVG TKRFGLDGGE AMIPALEAVI KYGGTLGVKE
IVYGMAHRGR LNVLANVLAK PYKVIFHEFS GGTANPEDVG GSGDVKYHLG TSADREFDGI
KVHMSLMPNP SHLETVDPVV LGKVRAYQTI ADDIGDDIGP GAKHKQVLPV LIHGDAAFAG
QGIIWECFGL SGVKGYNTGG CIHFIINNQI GFTTSPQFAR NSPYPSDVAK GVQAPILHVN
GDDPAAVTFA CKLAIDYRQT FGRDIVIDMW CYRRFGHNEG DEPGFTQPLM YQKIRQHPPV
SKIYGDRLKQ EGVIDDTFLA QTEAEFTAHL EDQFEAAKTY KANQADWFSG QWSGFHKPAD
PETARRNVDT TIENKLFDSL GRTLTTVPEG LTVHKTLARV LAAKEEMFKS GEGFDWATAE
ALAFGSLVTE GYNVRLSGQD CERGTFSQRH SVWVDQTDER KYTPLTTLPH GRFEVLNSTL
SEYGVLGFEY GFASADPKTL VLWEAQFGDF ANGAQIIIDQ YVASAESKWL RANGLVMLLP
HGYEGQGPEH SSARLERYLQ LCAQDNIQVC NITTPANYFH VLRRQMHRPF RKPLIIMTPK
SLLRHPLAKS AASEFTGGTF SRILSDPNGS EDAATKKVIL CSGKVFYDLL EARDAAEIDD
TQIIRIEQLY PFPGEPLAQR LSRMPNLEEV VWCQEEPQNN GSWFFVESQI EAAAKEAGVA
QPRPRYAGRN ASASPATGLA KRHVAEQAAL VADALHLSVR SELRRKQKA
//
