ID A0A0S8KZ39_9PROT Unreviewed; 951 AA.
AC A0A0S8KZ39;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:KPL27138.1};
GN ORFNames=AMJ72_10465 {ECO:0000313|EMBL:KPL27138.1};
OS Acidithiobacillales bacterium SM1_46.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703384 {ECO:0000313|EMBL:KPL27138.1, ECO:0000313|Proteomes:UP000052054};
RN [1] {ECO:0000313|EMBL:KPL27138.1, ECO:0000313|Proteomes:UP000052054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1_46 {ECO:0000313|EMBL:KPL27138.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL27138.1}.
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DR EMBL; LJVB01000101; KPL27138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KZ39; -.
DR PATRIC; fig|1703384.3.peg.192; -.
DR Proteomes; UP000052054; 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:KPL27138.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 602..795
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 951 AA; 105732 MW; F34438196096DE22 CRC64;
MDDTAKHTLH AWWRSSPLAV SNAPYLEALY ETFLRDPSGI DPVWQRYFET LPGAASGAPD
ISHEEIREQF RQLARARRTS PRAPEPAAAP DVAQKQVRVL QLINAYRFRG HQFASLDPLG
LREKQPLGEL DLRYHGLSDL DLDLRFDTGS LVGARRAPLR DILAQLQSTY CGSIGAEYMH
ITDTAEKRWL QSALESVHGV PPYPAETRRR LLERLTAAEG LEHYLHAKYV GQKRFSLEGG
ESLIPMLDEL IQRAGDSGVK EIVVGMAHRG RLNVLVNILG KTPAELFLEF EGKARSAAGT
GDVKYHKGFS SDIDTPGGPV HLALAFNPSH LEIVGPVVQG SVRARQERRH DKRGVRVLPV
VIHGDAAFAG QGVVMETFNL SQLRGYRTGG TVHIVINNQI GFTTSLTQDA RSTLYCTDVA
RMLNAPILHV NGDDPEAVLF ATEIALDYRS NFRKDVVLDL VCYRRHGHSE ADEPTVTQPT
MYQRIRELPT TRARYARHLT ETGVVTSEES DAMAKQFRDR LDAGDAVAPN LTPKGKSGYA
YGTDWSRFAR EATEDADTAV ALETLRALTE RLLLLPDGFE PHPSVAKVND ARRKMAAGAL
PIDWGYAETL AYATLLRQGY GVRLSGQDTG RGTFFHRHAI LHSRKDGEVF VPLRNLFEGQ
PDFRAINSPL TEEACLAFEY GYSTADPGTL VIWEAQFGDF ANNAQVVIDQ FISAGEQKWG
RLCGLTLLLP HGLEGQGPEH SSARLERYLQ LCAQQNMFVC SPTTPAQFFH LLRRQMLART
RKPLVVMTPK SLLRHRLAVS SLEDLTGGGF QTIVPEGDAL DPGSVTDVVM CSGKVYYDLV
EQRRERGATH AAILRIEQLY PFPEALLATE LGHYPRARRF VWCQEEHKNQ GAWYPSQHHI
WRVLPPGARL EYAGRPTSAA PAVGDYKLHL QELRELANNA LGLEGDKGKT A
//
