ID A0A0W1GSB9_9SPHN Unreviewed; 940 AA.
AC A0A0W1GSB9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:KTE57709.1};
GN ORFNames=ATE69_02595 {ECO:0000313|EMBL:KTE57709.1};
OS Sphingopyxis sp. H071.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759078 {ECO:0000313|EMBL:KTE57709.1, ECO:0000313|Proteomes:UP000054127};
RN [1] {ECO:0000313|EMBL:KTE57709.1, ECO:0000313|Proteomes:UP000054127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H071 {ECO:0000313|EMBL:KTE57709.1,
RC ECO:0000313|Proteomes:UP000054127};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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:KTE57709.1}.
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DR EMBL; LNSF01000001; KTE57709.1; -; Genomic_DNA.
DR RefSeq; WP_058455591.1; NZ_LNSF01000001.1.
DR AlphaFoldDB; A0A0W1GSB9; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000054127; 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:KTE57709.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 583..774
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 104310 MW; 1CC541A69E9B2F59 CRC64;
MNLERQSFDV DEVQAGPSWA PKNWPQIDSD DLTAALDPQQ MQVAVKAAAA KAGAPLSNAE
VERAANDSIR AMMLIRTYRV RGHLAANLDP LGLSTRELPA DLTPEYHGFV GADQDRPIWI
GGTLGLEKAT IREIVAILRA NYCGNVGLEY MHIADIEERQ FLQERMEGAD KIIEFSVEGK
RAILNKVIQA EEWEKFLARK YVGTKRFGLD GGESMIPAME SIIKYGGQYG VKEIVYGMAH
RGRLNMLANV MAKPYKVIFH EFAGGSANPD DIGGSGDVKY HLGTSTDREF DGISVHMSLV
PNPSHLEAVD PVVLGKVRAQ QVVRDDLDKH EQVLPVLIHG DAAFAGQGIV WECLGFSGIR
GYNTGGCIHF IVNNQIGFTT SPQFARSSPY PSDVAKGVQA PILHVNGDDP EAVTFACKLA
IDFRQRFKRD VVIDMWCYRR FGHNEGDEPS FTQPLMYERI RKHPPVSQLC AAKLEDEGAI
DAGWADARRA EFVAQLEGDF EAAKSYKPNK ADWFAGRWSG LYAPTDPEGA RRNIATGVSD
KLFDAIGRTL TTIPADLEVH KTLRRVIDGR AAMFADKSDT EIFDWATSEA LAFGTLLSEG
YQVRLSGQDS GRGTFSQRHA VWVDQKDEHK YIPLTTVPHG RFEVLDSPLS EYGVLGFEYG
YAMADPKSLV LWEAQFGDFA NGAQIMIDQF IAAGEAKWLR ANGLVMLLPH GYEGQGPEHS
SARLERFLQL CAGDNIQVCN ISTPSNYFHV LRRQMLRPFR KPLVIMTPKS LLRHKLAVSQ
RSDFIGDAHF RRIMSDRTPP ADADIKRVVL CSGKLGYDLM EARDAAGQTD TTVIRIEQIY
PFPGEPLAVR LKRMPKLEEV VWAQEEPRNN GSWFFVEPFI EEALKEAGFK GMRPRYAGRA
AAASPATGLM SRHQTEQSAL VADALGLSVR AEIRRAKNKA
//
