ID   A0A0W0Y7F9_9GAMM        Unreviewed;       745 AA.
AC   A0A0W0Y7F9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion {ECO:0000313|EMBL:KTD52550.1};
GN   ORFNames=Lqui_0116 {ECO:0000313|EMBL:KTD52550.1};
OS   Legionella quinlivanii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD52550.1, ECO:0000313|Proteomes:UP000054618};
RN   [1] {ECO:0000313|EMBL:KTD52550.1, ECO:0000313|Proteomes:UP000054618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD52550.1,
RC   ECO:0000313|Proteomes:UP000054618};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
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   -!- 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:KTD52550.1}.
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; LNYS01000003; KTD52550.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0Y7F9; -.
DR   STRING; 45073.Lqui_0116; -.
DR   PATRIC; fig|45073.5.peg.122; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000054618; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000054618};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          398..579
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   745 AA;  81628 MW;  C592F14EDA05C48D CRC64;
     MLDRASVVDE QFLKKIKAAD FPAALSNTQP GQAGLDKKLA IELFDSQIKS RLLDLIARQL
     KEKGLSFYTI GSSGHEGNAV FGQVFRPADM AFLHYRSGGF YLQRAKQVAG CDGVRDILLS
     LVAAAEEPIA GGRHKVFGSV PLSIPPQTST IASHLPKALG AAISITRARE LGIKSKLPAD
     SIVLCSFGDA STNHASSQTT LNACSWIASQ GYPLPLVFIC EDNGIGISVP TPNHWIESSI
     KNRPAIHYLS CDGLNIADTF LKAQEAQQIA RQKKQPVFLH MKCVRLLGHA GSDIESQYHS
     QAEIERIEAN DPLLHTARIL HEQDWMSLES MAELYLDNKS LIEAKAMEAV RLPRMSSAAE
     VMSSIIPKPT SATLYPVPDE AARIKAFGSA YNQLSLKRNL CQNINFALTD LMAQYPNMLI
     FGEDVGKKGG VYRVTADLQT RFGQRRVFDS ILDETTILGT AIGLSHNGFI PVPEIQFLAY
     LHNAEDQLRG EASTLSFFSN GQYCNPMVIR IAGLAYQKGF GGHFHNDNSI AVLRDLPGVI
     VACPSNGPDA AKMLRTCIKL AHEEGRVVVF LEPIALYMTK DLHENGDNGW LFEYPPAHET
     IAAGEVGVFG EGDTVILSYA NGYYLSRQAA KILRDQYQIK VKIVDLRWLS PLPAQAILRE
     VAKAKRVLIV DEGRRSASIS EGLTTLLAEE ASSRLKIKRI TGEDCFIPLG TAWQYLLPSK
     ESIVEAVLDL NSVKREKESG RLAVS
//