ID   U5BN61_9BACT            Unreviewed;       937 AA.
AC   U5BN61;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, 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   ORFNames=P872_06905 {ECO:0000313|EMBL:ERM81970.1};
OS   Rhodonellum psychrophilum GCM71 = DSM 17998.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Rhodonellum.
OX   NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM81970.1, ECO:0000313|Proteomes:UP000016843};
RN   [1] {ECO:0000313|EMBL:ERM81970.1, ECO:0000313|Proteomes:UP000016843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GCM71 {ECO:0000313|EMBL:ERM81970.1,
RC   ECO:0000313|Proteomes:UP000016843};
RX   PubMed=24309741;
RA   Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT   "Draft Genome Sequence of the Psychrophilic and Alkaliphilic Rhodonellum
RT   psychrophilum Strain GCM71T.";
RL   Genome Announc. 1:e01014-13(2013).
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:ERM81970.1}.
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DR   EMBL; AWXR01000036; ERM81970.1; -; Genomic_DNA.
DR   RefSeq; WP_019596684.1; NZ_KB906674.1.
DR   AlphaFoldDB; U5BN61; -.
DR   PATRIC; fig|1123057.7.peg.3165; -.
DR   eggNOG; COG0567; Bacteria.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000016843; 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:UP000016843};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          601..794
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          53..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   937 AA;  106495 MW;  4E77A5D0F8A4CC70 CRC64;
     MDKFSYIANA HVAYIDELYV EYKKNPESVD PSWKSFFDGF EFAITQYGED ENGGALKGTS
     MAEAEPSTTP TSSGSLATKG TIMDMELLPK EIKVRALIHA YRSRAHLRSK TNPVRERKDR
     KALIDLEDFG LDQQDLNTEF QAGKEIGIGT AKLSKIMEAL KTIYEGPMGF EYLYIRDPEM
     LDWFKTKVEK EALAFNPSVE EKKQILSKLN QAVVFENFLH TKYIGQKRFS LEGGESTIPF
     LDAVVNASAD LGVEEFMLGM AHRGRLNVLA NIMGKTYEQI FSEFEGTAKP DLTMGDGDVK
     YHMGYSSDLV TPNNKKIHLK LAPNPSHLEA VNPVVEGFIR AKIDSQHKGD SKKAMAILIH
     GDAAVAGQGI VYEVTQMAEL KGYNTGGTIH FVINNQVGFT TDFDDARSSI YCTDVAKIID
     APVIHVNGDN AEAVVFAARL ASEFRQKFNK DIFVDMVCYR RHGHNESDEP KFTQPSLYNI
     ISKHPNPREI YVKKLTERGD FDAKIAKQMD EEFRQLLQDR LNMVKEKPLP YQQTKFETVW
     ESLRRSTPED FELSPETGIS EETIKVVADA LTTIPKGFKP IKQIEVQLKQ RKDMFFNSKS
     LNWAAAELLA YGSLLKDGET VRITGQDCQR GTFSHRHAVV HDANTNTPHN FLKELKGHDG
     KFYIYNSLLS EYAVLGFEYG YGMANPHSLT VWEAQFGDFA NGAQTMIDQF ITSGESKWQK
     MNGLVMLLPH GYEGQGPEHS NARPERFLQL SAEYNIIVAN ITEPSNFFHL LRRQLAWEFR
     KPCVVMSPKS LLRHPKVMSP ISEFTNGRFR EIILDTKTNP DEVKRVVLCS GKIYYDLEEV
     REKEKVTDVA IIRIEQLHPL PKKQMFEALK QYKNAEVFWV QEEPENMGYW NYLLRLLYKE
     LPMELIARKN SASPATGYNK VHVEEQTAIV RKALKLS
//