ID A0A0J5GGH6_9NEIS Unreviewed; 942 AA.
AC A0A0J5GGH6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=sucA {ECO:0000313|EMBL:KMJ53417.1};
GN ORFNames=ACG97_07850 {ECO:0000313|EMBL:KMJ53417.1};
OS Vogesella sp. EB.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ53417.1, ECO:0000313|Proteomes:UP000054352};
RN [1] {ECO:0000313|EMBL:KMJ53417.1, ECO:0000313|Proteomes:UP000054352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB {ECO:0000313|EMBL:KMJ53417.1,
RC ECO:0000313|Proteomes:UP000054352};
RA Arrua Day P., Revale S., Alvarez H.M.;
RT "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT Vogesella sp. strain EB.";
RL Submitted (JUN-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 -!- 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:KMJ53417.1}.
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DR EMBL; LFDT01000010; KMJ53417.1; -; Genomic_DNA.
DR RefSeq; WP_047966802.1; NZ_LFDT01000010.1.
DR AlphaFoldDB; A0A0J5GGH6; -.
DR STRING; 1526735.ACG97_07850; -.
DR PATRIC; fig|1526735.3.peg.1684; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000054352; 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; IPR032106; 2-oxogl_dehyd_N.
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; PF16078; 2-oxogl_dehyd_N; 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:KMJ53417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054352};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 594..791
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 942 AA; 105701 MW; EB1EB869293629D1 CRC64;
MMQSMYSHSY LFGGNAPFIE DLYEQYLADP TVVSPEWRDY FDKLSTAPGA ADRDVAHQPI
QESFIQLAKR PPVAQRSSAA TDWESMQKQV AVLKLISAYR VLGSRQANLD PLKRMDQATL
RELDHATHGL TDADMAVHFN VGSLVAPQKL PLSEIIARLK QTYCGNIGVE YMHITNSEEK
HWVQKRFEGD LSTPHYNADK KKRIFKQITA AETLERYLHT KYVGQKRFSL EGGESAIAAL
DHLIQNATSV GVEELIIGMA HRGRLNVLVN TLGKQPRDLF AEFEGKAAQE LASGDVKYHM
GFSSDIPTAN GPMHVSLAFN PSHLEIVNPV VEGSVRARQD RRKDSERKAA VPVLIHGDSA
FAGLGVNQGT FNLSQTRGYG TGGTLHIVIN NQVGFTTSDT RDMRSTLYCT DVAKMIEAPI
FHVNGDDPEA VCYVMQAALD FRMKFNKDVV IDLVCYRKLG HNEGDDPFLT QPMMYKKIAK
HGGVRAMYAE RLVGEGVLTA AEADNFIQAY RDALDKGEHV EQTVLSNYRR EHALDWSQYQ
GTHWAHPTDT SLPHADIQRL AEKFTSVPEN YKLHPTVKRV QDARRAMAAG EQAIDWGMAE
TLAYASLVTN GYGVRISGED SGRGTFSHRH AVVHDQNRER WDQGTYVPLR NMSDNQADFL
VIDSILNEEA VLAYEYGYAC SAPDQLVIWE AQFGDFANGA QVAIDQFISS GETKWGRLCG
LTTILPHGYD GQGPEHSSAR LERWLQLCAE HNMQIVMPSE ASQMFHVLRR QVLRPFRKPL
VIFLSKRLLR YKDAMSPLED FTSHSFRPVI GDAGISDAKA VKRVILCSGQ VYYDLVNGRK
ERELDSEVAI IRVEQLYPFP TEQLQAELAR FSHVKEIMWV QEEPRNQGAW YQIRHRLEAL
LGAKQTLLFA GRPSSASPAV GYMSKHVAQL KGFIEEAMSV NK
//
