ID A0A0R0E2U8_9GAMM Unreviewed; 943 AA.
AC A0A0R0E2U8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:KRG84490.1};
GN ORFNames=ABB33_11520 {ECO:0000313|EMBL:KRG84490.1}, AOT14_23280
GN {ECO:0000313|EMBL:ALJ28696.1};
OS Stenotrophomonas acidaminiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=128780 {ECO:0000313|EMBL:KRG84490.1, ECO:0000313|Proteomes:UP000050958};
RN [1] {ECO:0000313|EMBL:ALJ28696.1, ECO:0000313|Proteomes:UP000061010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZAC14D2_NAIMI4_2 {ECO:0000313|EMBL:ALJ28696.1,
RC ECO:0000313|Proteomes:UP000061010};
RX PubMed=26659678;
RA Vinuesa P., Ochoa-Sanchez L.E.;
RT "Complete Genome Sequencing of Stenotrophomonas acidaminiphila
RT ZAC14D2_NAIMI4_2, a Multidrug-Resistant Strain Isolated from Sediments of a
RT Polluted River in Mexico, Uncovers New Antibiotic Resistance Genes and a
RT Novel Class-II Lasso Peptide Biosynthesis Gene Cluster.";
RL Genome Announc. 3:e01433-15(2015).
RN [2] {ECO:0000313|EMBL:KRG84490.1, ECO:0000313|Proteomes:UP000050958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13310 {ECO:0000313|EMBL:KRG84490.1,
RC ECO:0000313|Proteomes:UP000050958};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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; CP012900; ALJ28696.1; -; Genomic_DNA.
DR EMBL; LDJO01000032; KRG84490.1; -; Genomic_DNA.
DR RefSeq; WP_054666599.1; NZ_LDJO01000032.1.
DR AlphaFoldDB; A0A0R0E2U8; -.
DR KEGG; sacz:AOT14_23280; -.
DR PATRIC; fig|128780.6.peg.2345; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000050958; Unassembled WGS sequence.
DR Proteomes; UP000061010; 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 ECO:0000313|EMBL:KRG84490.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 595..788
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 943 AA; 103974 MW; 201303BC8BE691D1 CRC64;
MDNLLKQFAQ SSQLAGGNAS YIEDLYEQYL VSPDSVDPKW KSYFDGFKGR EAGDVPHSAV
IAHIAEAGRN ASSAVAGSGG GDERERNVGR LITAYRSRGH LGAQLDPLGL TPPVNPPDLG
LAFHHLSDAD LNDEFSTGGV GGQPRMKLRD LLARLKATYT GSIGAEFMYI AEVDQRQWLY
QRLENAGGNY NLDADTQRRT LERLTAAEGL ERYLHTKYVG QKRFSLEGGD SLIPMMDTVI
RGAGKDGVKD VVIGMAHRGR LNVLVNTLGK NPRKLFDEFE GRFEHDDRAV AGDVKYHMGF
SADVATAGGP VHLALAFNPS HLEIVDPVVA GSVRSRQERR GDAARKQVMP ILIHGDAAFA
GQGVVMELFQ MSQARGFAVG GTVHIVINNQ VGFTTSNRDD SRSTLYCTDI AKMVGAPVLH
VNGDDPEAVV FAAQLAYDFR QQFHKDVVID LVCYRRWGHN EADEPAITQP LMYQVIRKHK
TTRELYAEKL EAAGVIPANG GKALVDAYRD KLDSGEVTTE LAQVEKTPPT SKLYVDWPKL
LAGKLSDPVS TQVPMAELAR LAKLINTIPE GVELHSRVAK VYDDRRRMAA GEIPGDWGFA
ENLAYATLLD QGHGLRLVGQ DVGRGTFTHR HAILHDQKTD AYYLPLRQLV QSPEQATIID
SLLSEEAVMA YEYGFSTTDP NTLCIWEGQF GDFANGAQVV IDQFIASGEA KWGRISGLTL
LLPHGYEGQG PEHSSARLER FLQLCALENM LVCVPSTPAQ AFHMLRRQLC MTTRKPLVVM
SPKSLLRHKL AVSTLDELAN GEFQHLIGDA NADAKKVKRV VLCSGKVYYD LLEDQTKRGQ
DDVAIIRVEQ LYPFPRTLLA AELNKYGKAA DVVWCQEEPM NQGAWYQIRH HLQACLADGQ
NLHYAGRPRS PSPAVGHMAD HLRELQQLLA DALVNPFNDQ FAE
//
