ID   A0A078KSE8_9GAMM        Unreviewed;       935 AA.
AC   A0A078KSE8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
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:CDZ75887.1};
GN   ORFNames=BN59_00147 {ECO:0000313|EMBL:CDZ75887.1};
OS   Legionella massiliensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ75887.1, ECO:0000313|Proteomes:UP000044071};
RN   [1] {ECO:0000313|EMBL:CDZ75887.1, ECO:0000313|Proteomes:UP000044071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUN-2014) 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};
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DR   EMBL; CCSB01000001; CDZ75887.1; -; Genomic_DNA.
DR   RefSeq; WP_043872522.1; NZ_CCVW01000001.1.
DR   AlphaFoldDB; A0A078KSE8; -.
DR   STRING; 1034943.BN59_00147; -.
DR   eggNOG; COG0567; Bacteria.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000044071; 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   Reference proteome {ECO:0000313|Proteomes:UP000044071};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          592..786
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   935 AA;  104604 MW;  D7D478FFDDCFD00B CRC64;
     MSSTDLQNQW ATSYLSGGSM AYVDALYEDF LADPNSVPAD WRAAFEALPT VNGGVKDVSH
     REIRDYFLEN ADKKQAAVVI SEDSKQYQVA HLMNAYRSHG HHAAKLDPLG MAERMHVPSL
     ELAYHQLSEA DMGRKFFAGK SFNGAQMSLR DIYQALRDTY CGSIGIEYMH ISDNAETEWL
     QEKMESVRGR PTFDANRKRT ILNDLIAADG LERYLGTRYV GQKRFSLEGG DAFIPMMKEI
     IRQGGNVGVK EIVIGMAHRG RLNVLVNVLG KEPSQLFQEF EGKIKSERTG DVKYHMGFSS
     DLRTEDGAVV HLALAFNPSH LEIIGPVVEG SARSRLRRQH DLDKKDKVVP VVIHGDAAFA
     GQGVVMETFN FSQARGYSTG GTIHIVINNQ VGFTTSNPLD ARSTLYCTDV AKMVQAPVLH
     VNGDDPEAVV FATQIAFEFR MKFKRDIVLD LVCYRRHGHN EADEPSVTQP TMYLKIKSMP
     TLREIYAEQL IANGLIKKEE VDNLVESYRD RLDKGQAVVD VVQGDYEGKV AVDWTPYINA
     KWTDKADTTI SKSTIQSLAK QLNQLPANFE LHPVVKRLLA DRDKMTSGEL PMNWGYAETM
     AYASLLAEGY GVRLSGQDSG RGTFAHRHAV LHDGKTGNTY VPLEKTASNP EKPFAVIDSV
     LSEEAVLAFE YGYASSEPRS LVLWEAQFGD FANGAQVVID QFISSGEQKW GRLCGLVMLL
     PHGYEGQGPE HSSARLERYM QLCAQHNMQV CTPTTPAQIF HLLRRQMIRK FRKPLIVMTP
     KSLLRHKLAV SPLEDLTKGK FQTVIPEVDD LNAAKVTKVV LCCGKVYYDL LQRRRDDKKL
     SHVAIIRVEQ LYPFPKKTLI QELEKYPNAK SVVWCQEEPQ NQGVWFATQH NIVACLRADQ
     SLSYAGREFA ASPAVGSPIL HAQQQQALVE QALLD
//