ID A0A2C6DNI6_9GAMM Unreviewed; 936 AA.
AC A0A2C6DNI6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:VFS49333.1};
GN ORFNames=CRN84_13420 {ECO:0000313|EMBL:PHI30263.1}, NCTC12282_03804
GN {ECO:0000313|EMBL:VFS49333.1};
OS Budvicia aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Budvicia.
OX NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI30263.1, ECO:0000313|Proteomes:UP000224974};
RN [1] {ECO:0000313|EMBL:PHI30263.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_387 {ECO:0000313|EMBL:PHI30263.1};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000224974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VFS49333.1, ECO:0000313|Proteomes:UP000373449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12282 {ECO:0000313|EMBL:VFS49333.1,
RC ECO:0000313|Proteomes:UP000373449};
RG Pathogen Informatics;
RL Submitted (MAR-2019) 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; PDDX01000001; PHI30263.1; -; Genomic_DNA.
DR EMBL; CAADJA010000002; VFS49333.1; -; Genomic_DNA.
DR RefSeq; WP_029094032.1; NZ_PDDX01000001.1.
DR AlphaFoldDB; A0A2C6DNI6; -.
DR STRING; 1111728.GCA_000427805_00883; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000224974; Unassembled WGS sequence.
DR Proteomes; UP000373449; 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:VFS49333.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000224974};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 594..787
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 936 AA; 105945 MW; ADB149113D7D0EF5 CRC64;
MQNGAIKTWL DSSYLAGANQ SYIEQLYEDY LTDPDSIDDS WRAIFDKLPI ENLSPDQFHS
TTRDYFRRLA KDSKRYTSSV SDPENDAKQV KVLQLINAFR FRGHQNANLD PIKLRYKEPV
LELDPAFHNL TEEDMQETFN VGSFAVGKET MKLSEIYQAL KQTYCDSIGA EYMHITNTEE
KRWIQQRLES VSGRGSFSVE EKKRFLRELT AAEGLERYLG AKYPGAKRFS LEGGDALIPM
LKEMVRHAAH NDGREVVLGM AHRGRLNVLI NLLGKRPGDL FDEFAGIHKE HLGTGDVKYH
QGFSSDFETD GKLVHLTLAF NPSHLEIVSP VVIGSVRARR DRIDATGSSN QVLPITIHGD
AAVIGQGIVQ ETLNMSQVRA YEVGGTVRIV INNQIGFTTS YPQDVRSTEY CTDIAKMIQA
PIFHVNADDP EAVAFVTRLA LDYRNTFKRD VMIDLVCYRR HGHNEADEPS ATQPMMYQKI
KKQPTPRKVY ADKLIETNVV SAQEVTEMVN LYRDALDNGD CVVEEWRPID THSMAWAPYL
NHEWDEEYPS SVEMKRLQDL AKRISQVPDN VELHPRVVKI YDDRALMADG EKPFDWGAAE
NLAYATLVDE NIPVRISGED SGRGTFFHRH AVVHNQKDGS YYIPLANVHN SQGNFQVWDS
VLSEAGVLAF EYGYATAEPR TLTIWEAQFG DFANGAQVVI DQFISSGEQK WGRMCGLVML
LPHGYEGQGP EHSSARLERY LQLCAEQNIQ VCVPSTPAQV YHMLRRQALR GMRRPLIVMS
PKSLLRHPLA ISSLDELANG VFQPAIGEID NLNPAQVKRV VMCSGKVYYD LLDQRRANGQ
SDVAIIRIEQ LYPFPHQVMQ NALLDYAHVK DFVWCQEEPL NQGAWYCSQH NIRDVIPEGS
KLRYAGRPAS ASPAVGYMSV HQEQQKNLVE DALNVK
//
