ID A0A0Q8RAI4_9SPHN Unreviewed; 692 AA.
AC A0A0Q8RAI4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN ORFNames=ASE22_02130 {ECO:0000313|EMBL:KRB94751.1};
OS Sphingomonas sp. Root720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB94751.1, ECO:0000313|Proteomes:UP000051570};
RN [1] {ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB94751.1, ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|EMBL:KRB94751.1,
RC ECO:0000313|Proteomes:UP000051570};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KRB94751.1}.
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DR EMBL; LMID01000001; KRB94751.1; -; Genomic_DNA.
DR RefSeq; WP_056354288.1; NZ_LMID01000001.1.
DR AlphaFoldDB; A0A0Q8RAI4; -.
DR STRING; 1736595.ASE22_02130; -.
DR Proteomes; UP000051570; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 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 Pyruvate {ECO:0000313|EMBL:KRB94751.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051570}.
FT DOMAIN 374..548
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 692 AA; 75072 MW; 475E9C68BE65E343 CRC64;
MATAAIQPPL RNAPDDTVDW KRVAYLVHLS RALDKMEETR LVPEKEVLYQ FSARGHDMGQ
ILLGCRLDNP QDASCGYYRS RPLLLALGVD VADALGSAMG RAGGYSDGRD IGVVFNFPNP
NGASALPMCG GVGAQYTPTA GWAQAIEYYR TVVKDPAYDK ALAVVLGGDG SVASNGFWAA
LTIATTQTLP MLFYIEDNGF GISVPSTFQT PGGNIAANLA SWQGLKIFSG DGTDPAEAAR
LVDEATAYVR DERAPAMLRL TVPRLQGHSF QDTQTYKSAN IVEAEWARDP LPKLKSYLVP
AVLGEDEWTA LEGEAQAAAE AACEEAKARP VSLPESVMKN VFFEGELQAE GGMALHGYVA
PASTEAAKPE GQRINMVTAI RRTLDHELSI NDKVVLFGED IGPKGGVHAV TLGLQEKYGT
SRVFDTSLSE EGIIGRAVGM ALAGLMPVPE IQFRKYAEPA TEQINDCGTM RWRTNNRFAA
PMVVRIPGGF FKCGDPWHSQ TNEVAFVHNP GWKVAVPSNA EDAVGLLRAS LRGNDPVIFF
EHRNLLDLAW ARRPYPGDDF VLPFGKAKLT RQGSDITIVT WGAMVPRCED AAAHVSADVI
DLRTLMPWDR EAVLDSVRRT RRCLIVHEDL QTAGFGAEIA AVVADEAFMD LDAPVARVTM
PDIPSPHNPL LLDWAVPSVE RIRAKIDELI AF
//
