ID   F2IVD0_POLGS            Unreviewed;       995 AA.
AC   F2IVD0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   Name=sucA {ECO:0000313|EMBL:ADZ72648.1};
GN   OrderedLocusNames=SL003B_4231 {ECO:0000313|EMBL:ADZ72648.1};
OS   Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Polymorphum.
OX   NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ72648.1, ECO:0000313|Proteomes:UP000008130};
RN   [1] {ECO:0000313|EMBL:ADZ72648.1, ECO:0000313|Proteomes:UP000008130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC   {ECO:0000313|Proteomes:UP000008130};
RX   PubMed=21478361; DOI=10.1128/JB.00333-11;
RA   Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT   "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT   degrading bacterium from oil-polluted saline soil.";
RL   J. Bacteriol. 193:2894-2895(2011).
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}.
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DR   EMBL; CP002568; ADZ72648.1; -; Genomic_DNA.
DR   RefSeq; WP_013654946.1; NC_015259.1.
DR   AlphaFoldDB; F2IVD0; -.
DR   STRING; 991905.SL003B_4231; -.
DR   KEGG; pgv:SL003B_4231; -.
DR   PATRIC; fig|991905.3.peg.4363; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000008130; Chromosome.
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:UP000008130};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          641..834
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   995 AA;  111956 MW;  3FD8A486DFC80EDE CRC64;
     MARQDANNVF ALTSFLYGAN AAYIEELYAQ YQENPASLDP EWQDFFGALQ DEKADVLREA
     RGAPWKRADW PLPAHGDLVN AFDGNWAPVE KALGDKLKKQ AEAKGARLSD ADVHQATRDS
     VRALMMIRAY RMRGHLHADL DPLRLSPPGD HEELHPSSYG FSDEDWDRPI FIDHVLGLEY
     ATIREMLEIL KRTYCSTLGV EFMHISDPAA KAWIQERIEG PDKHVEFTPR GKRAILNKLV
     EAEGFEKFLD VKYTGTKRFG LDGGEALIPA LEQIIKRGGQ MGLKEIVLGM AHRGRLNVLS
     QVMAKPHRAI FHEFKGGSYA PDDVEGSGDV KYHLGASSDR SFDGNDVHLS LTANPSHLEI
     VNPVVLGKAR AKQDQHSAVD GHWVTDTTTI DRSKVLPLLL HGDAAFAGQG VVAECFGLSA
     LRGHRTGGSI HVIINNQIGF TTNPRFSRSS PYPSDVAKVI EAPIFHVNGD DPEAVVYAAK
     IATEFRQIFG RPVVIDMICY RRFGHNEGDE PAFTQPIMYR KIRKHPTTLQ IYADRLIAEG
     VITAEEVEEL KAAWRKHLDE EFEAGQTYKP NKADWLDGKW AGLKRAADEE DPRRGSTGVP
     VSELKEIGRR LSTVPDGFNV HRTIGRFMSN RAAMIETGEG IDWATAEALA FGSLLREGHP
     VRLSGQDCER GTFSQRHSVL YDQEDEGRYI PLNHLSDDQA RYEVINSMLS EEAVLGFEYG
     YSLAEPKALT LWEAQFGDFA NGAQVLFDQF ISSGERKWLR MSGLVCLLPH GYEGQGPEHS
     SARLERYLQL CAEDNMQVAN CTTPANYFHI LRRQLKRDIR KPLILMTPKS LLRHKRAVST
     LAELGETSSF HRLLWDDAQY LADSPVKLVA DDKIRRVVMC SGKVYFDLYE EREKRGIDDV
     YLLRVEQLYP FPKKALAQEL ARFRNADMVW CQEEPKNMGG WTFVEPYIEW VLTEVGHKVR
     RPRYAGRAAM ASTATGLMSQ HLAQLQAFLD EAFAD
//