ID A0A099KED2_9GAMM Unreviewed; 932 AA.
AC A0A099KED2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=ND16A_2408 {ECO:0000313|EMBL:KGJ88706.1};
OS Thalassotalea sp. ND16A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ88706.1, ECO:0000313|Proteomes:UP000029848};
RN [1] {ECO:0000313|EMBL:KGJ88706.1, ECO:0000313|Proteomes:UP000029848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND16A {ECO:0000313|EMBL:KGJ88706.1,
RC ECO:0000313|Proteomes:UP000029848};
RA Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA Hazen T.C.;
RT "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT Eastern Mediterranean Deep Water.";
RL Submitted (AUG-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};
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:KGJ88706.1}.
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DR EMBL; JQDZ01000114; KGJ88706.1; -; Genomic_DNA.
DR RefSeq; WP_033079020.1; NZ_JQDZ01000114.1.
DR AlphaFoldDB; A0A099KED2; -.
DR STRING; 1535422.ND16A_2408; -.
DR PATRIC; fig|1535422.3.peg.3506; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000029848; 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:KGJ88706.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029848};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 591..784
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 932 AA; 105317 MW; B609C72ED76CC2A5 CRC64;
MPEGAMKAWL ESSHFSGNNA EYIEELYESY LENAHSVADE WRKVFDQLPK VEGVEVETNH
SVVRDEFRQL AKEGVKHVAV SSEADAKQVR VLQLINAYRF RGHQNARLDP LGLWQRERVR
DLELQHHDLS KSEFDKEFNV GSLAVGHESM RLGDIYKTLE KTYCGSIGAE YMHITSTTEK
RWLQQRLESV QAQANFSVEQ KTELLKDLIA ADGLEKYLGA KFPGAKRFSL EGGDSLIPML
KQLITRAGEH GTKEVVLGMA HRGRLNVLVN VMGKNPSKLF DEFAGKVEQM GSGDVKYHQG
YSSDFITPGG AVHLALAFNP SHLEIVNPVV IGSVRARLDR RDCDKGDLVL PITIHGDSAI
AGQGVVQETF NMSQARAYKV GGTIRIVVNN QVGFTTSKQE DTRSTEYCTD IAKMVQAPIL
HVNGDDPEAV ILATQIALDY RNTFKRDVVI DLVCYRRHGH NEADEPNATQ PLMYQKIKKH
PTPRQLYADQ LDAERSITAA QNKEFVEYYR KLLDEGQCTV EQWRPMTEHS VDWTPYIGHD
WDDDYDHQIP VSKLKELAVN ISTYPEQHKL QSRVKKIYDD RKKMAAGEKM LDWGFAENLA
YAAIVEQGER VRITGQDAGR GTFFHRHSVL HNQDDASTYL PLQHISKEQG PFEVYDSVLS
EVAVLAFEYG YTTAEPSGLT IWEAQFGDFA NGAQVVFDQF ISSGEQKWGR LCGLTILLPH
GYEGQGPEHS SARLERFLQL CADHNMQVCV PSTPAQVFNM LRRQVVRPMR RPLIVMSPKS
LLRHPLAVSS LEELADGTYH NVIGEIDELN AKDVTRVVMC SGKVYYELLE QRRKNEQKDV
AIVRIEQLYP FPEAELKDVF ALYPNAKDFV WCQEEPQNQG AWYCSQHHFR STIPQGSTLT
YAGRTASAAP ACGYMSLHVK EQQALVNDAL NK
//
