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Database: UniProt
Entry: G8U071_SULAD
LinkDB: G8U071_SULAD
Original site: G8U071_SULAD 
ID   G8U071_SULAD            Unreviewed;       946 AA.
AC   G8U071;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:AEW05320.1};
DE            EC=1.2.4.2 {ECO:0000313|EMBL:AEW05320.1};
GN   OrderedLocusNames=Sulac_1827 {ECO:0000313|EMBL:AEW05320.1};
OS   Sulfobacillus acidophilus (strain ATCC 700253 / DSM 10332 / NAL).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX   NCBI_TaxID=679936 {ECO:0000313|EMBL:AEW05320.1, ECO:0000313|Proteomes:UP000005439};
RN   [1] {ECO:0000313|Proteomes:UP000005439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700253 / DSM 10332 / NAL
RC   {ECO:0000313|Proteomes:UP000005439};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA   Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R.,
RA   Gehrich-Schroeter G., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of chromosome of Sulfobacillus acidophilus DSM
RT   10332.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEW05320.1, ECO:0000313|Proteomes:UP000005439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700253 / DSM 10332 / NAL
RC   {ECO:0000313|Proteomes:UP000005439};
RX   PubMed=23407703; DOI=10.4056/sigs.2736042;
RA   Anderson I., Chertkov O., Chen A., Saunders E., Lapidus A., Nolan M.,
RA   Lucas S., Hammon N., Deshpande S., Cheng J.F., Han C., Tapia R.,
RA   Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N., Mikhailova N.,
RA   Pati A., Palaniappan K., Land M., Pan C., Rohde M., Pukall R., Goker M.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Mavromatis K.;
RT   "Complete genome sequence of the moderately thermophilic mineral-sulfide-
RT   oxidizing firmicute Sulfobacillus acidophilus type strain (NAL(T)).";
RL   Stand. Genomic Sci. 6:1-13(2012).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP003179; AEW05320.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8U071; -.
DR   STRING; 679936.Sulac_1827; -.
DR   KEGG; sap:Sulac_1827; -.
DR   PATRIC; fig|679936.5.peg.1892; -.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   Proteomes; UP000005439; 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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
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; 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   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AEW05320.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005439};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          592..787
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          911..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..931
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   946 AA;  105573 MW;  72468F0FD7D4D997 CRC64;
     MDTQQVFEWF VGPNLGYLAE AYERYRNDPD SVDPETRALI EQLDPAWWER WLGGETTAQP
     VAGPTTTIPT EKIVKAVQLA RTIREFGHLQ ASFDPLGVSP RKVVDDPEVM GITDNDLAQM
     PATVVWPRGL RQAPNALEAV KILRQVYSGP LGYDFSHVHN FDERDWLRQQ VEGGGLTVSF
     SPEEKRALLF RLTEVEGFER FLHTTFPGQK RFSIEGTDML VPMLDSLIAQ AVKQGIHEVT
     IGMAHRGRLN VLAHILGKPY EKIFSEFHSA PNKELVPSEG SMGINAGWTG DVKYHLGAHK
     LLRDGELSGA RITLANNPSH LEFVNPVIQG ATRAAQEDTR HPGQPSLEVD RAMAIAIHGD
     ASFPGEGIVA ETLNLSRLAG YHTGGTVHII MNNGLGFTTG PEEGRSTLYA SDLAKGYEIP
     VVHVNADDPM ACLLAVQLAF EYRQRFHKDF LIDLVGYRRW GHNEGDEPAY TQPVLYQKIA
     RHPTVRALFA DRLVSEGIVT PEEVQEMAGQ VHARLVEAKD RVQDGVIPPD EPEPSTWSDA
     LIALAEPTAV DADELIRLAR EAHQWPEAFH PNPKLARQLQ RRLDNLTEPN GIDWGLAETL
     AFASILAEGT PIRLSGQDSE RGTFSQRHLV LHDVDTNQKY TPLQHLPSAR ASFAVYNSPL
     SEAAVLGFEY GYNVEAPTVM TLWEAQFGDF ANAAQVIIDQ FLSAARAKWK ERSGLVLLLP
     HGYEGQGPEH SSARLERYLQ LAADNNMRIA NCTTAAQYFH LLRQQSHLLR RDPRPLVIMT
     PKSLLRHPLA ASSLHDLSHG RFQPVLEHEA AKEHPESIER VILLSGKVVV DVLTRLGGHV
     PEHVSIIRLE QLYPFPDGEI EAIFHRYPNL TDVVWLQEEP RNMGAWRYIQ PRLEAHLPPG
     RTLRYAGRPE RAATAEGFPE MHEEEQGRIV QDALGESKVS TQGGHR
//
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