ID A0A246JIU5_9SPHN Unreviewed; 940 AA.
AC A0A246JIU5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, 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 ORFNames=CDQ92_20255 {ECO:0000313|EMBL:OWQ92492.1};
OS Sphingopyxis bauzanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=651663 {ECO:0000313|EMBL:OWQ92492.1, ECO:0000313|Proteomes:UP000197361};
RN [1] {ECO:0000313|EMBL:OWQ92492.1, ECO:0000313|Proteomes:UP000197361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22271 {ECO:0000313|EMBL:OWQ92492.1,
RC ECO:0000313|Proteomes:UP000197361};
RX PubMed=20023054; DOI=10.1099/ijs.0.018218-0;
RA Zhang D.C., Liu H.C., Xin Y.H., Zhou Y.G., Schinner F., Margesin R.;
RT "Sphingopyxis bauzanensis sp. nov., a psychrophilic bacterium isolated from
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 60:2618-2622(2010).
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:OWQ92492.1}.
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DR EMBL; NISK01000009; OWQ92492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246JIU5; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000197361; 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 Reference proteome {ECO:0000313|Proteomes:UP000197361};
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; 104229 MW; 257F8B1A57A44EFD CRC64;
MNLERQSFDI DEPQAGPSWA PKNWPPVDSD DLTAALDPQQ MQVAVKAAAA KGGAPLSNAE
VERAANDSIR AMMLIRTYRV RGHLAANLDP LGLSQRELPA DLTPEYHGFV GADQDRPVWL
GGTLGFERAT VRELVAVLRA NYCGNVGLEY MHIADLKERQ FLQERMEGAD KIIEFSVEGK
RAILSKVIEA EEWEKFLAKK YVGTKRFGLD GGESMIPAME AIIKYGGQYG VKEIVYGMAH
RGRLNMLANV MAKPYKIIFH EFAGGSANPD DIGGSGDVKY HLGTSTDREF GGASVHMSLV
PNPSHLEAVD PVVLGKVRAQ QVVRDDLTKH EQVLPVLIHG DAAFAGQGIV WECLGFSGIR
GYNTGGCIHF IVNNQIGFTT SPQFARSSPY PSDVAKGVMA PILHVNGDDP EAVTFACKLA
IDFRQQFKRD VVIDMWCYRR FGHNEGDEPS FTQPLMYARI RQHPPVSQLC AAKLESEGVI
DAGWADARRA EFIARLEDDF EGAKSYKPNK ADWFAGRWSG LHAPADPENS RRNIATGVSE
KLFDSIGRIM TSVPDDLDVH KTLRRVIDAR GAMFADKSDK EVFDWATAES LAFGTLLSEG
YQVRLSGQDS GRGTFSQRHA VWVDQKDERK YVPLTTVPHG RFEVLDSPLS EYGVLGFEYG
YAMADPKSLV LWEAQFGDFA NGAQIMIDQF IASGEAKWLR ANGLVMLLPH GYEGQGPEHS
SARLERFLQL CAGDNIQVCN ISTPSNYFHV LRRQMLRPFR KPLIIMTPKS LLRHKLAVSQ
RSDFIGEAHF RRIMSDRTAL EDKDVKRVVL CSGKVAYDLM EARDAAGQTD TTVIRIEQLY
PFPGEALSVR LKRMPKLEDV VWAQEEPRNN GGWSFVEPFI EDALTAADKK GMRPRYAGRT
AAASPATGLM SRHQTEQAAL VADALGLSVR AEIRRSKNKA
//
