ID F6F3N2_SPHCR Unreviewed; 671 AA.
AC F6F3N2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
DE AltName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=Sphch_3452 {ECO:0000313|EMBL:AEG51044.1};
OS Sphingobium chlorophenolicum L-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG51044.1, ECO:0000313|Proteomes:UP000007150};
RN [1] {ECO:0000313|EMBL:AEG51044.1, ECO:0000313|Proteomes:UP000007150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-1 {ECO:0000313|EMBL:AEG51044.1,
RC ECO:0000313|Proteomes:UP000007150};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT "Complete sequence of chromosome 2 of Sphingobium chlorophenolicum L-1.";
RL Submitted (MAY-2011) 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 -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002799; AEG51044.1; -; Genomic_DNA.
DR RefSeq; WP_013849274.1; NC_015594.1.
DR AlphaFoldDB; F6F3N2; -.
DR STRING; 690566.Sphch_3452; -.
DR KEGG; sch:Sphch_3452; -.
DR HOGENOM; CLU_012907_2_1_5; -.
DR Proteomes; UP000007150; Chromosome 2.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEG51044.1}; Pyruvate {ECO:0000313|EMBL:AEG51044.1}.
FT DOMAIN 344..519
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 671 AA; 71205 MW; 53F94F1EACEB0F90 CRC64;
MTSTNSSAIL SDASYARHSL AQIAFIRAFE AKALALTQTK PPSVLGSMHF CAGQEAVPLG
AVAGLRDDDQ IVCTYRGHGW AIASGLDPRA VFAEICQKAE GINGGRAGSA LMMAPDTRFI
GENSIVGAGT TIACGVAMAN LHKGNGRVVV VTIGDGALNQ GAVSEAFALA AARKLPVIFV
VENNGWSEMT STDDMFLAKR LAQRTAGYGI PSATIHGTDP IVVRDSFAIA AERARNGDGP
VLLECRVPRL WGHYNRDMEH YRSKEDRRKA EQIDPFITLS QRMIDAGLMT EREVEELREE
EERKVERIAD VVMASPDPVP EGLLDHVVAA PTDGRPRVTG TKEMSFIEAV NAALRAELDN
DEAVIVYGED VGKGGGIFAA SRNLQREYGA HRVFDTPIAE NAILGSAVGA AISGLKPIVE
IMWADFLFVA LDQLVNQASN IRYITGGKSG APMVVRTQQG ATPGSCAQHS QSIEAMLAHV
PGLKVALASS ATDAYALLRA ASADPDPVIV IEARGLYQVR STVELTEGAE PVGKARLRRP
GKDVAIISWG TMVDPAEAAA EALAEEGIDA AVLDLRWLNP IDEEALAHVV GEAGGRVLIV
HEAVRTGGFA GEIGFRIQEL LGERMALSVR RLATMDTRIP ASPVLQAAVI PNARSIANVA
RALAGKRMIA A
//
