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Database: UniProt
Entry: A0A167YY11_9BACI
LinkDB: A0A167YY11_9BACI
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ID   A0A167YY11_9BACI        Unreviewed;       947 AA.
AC   A0A167YY11;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|HAMAP-Rule:MF_01169, ECO:0000256|SAAS:SAAS00010308};
DE            EC=1.2.4.2 {ECO:0000256|HAMAP-Rule:MF_01169, ECO:0000256|SAAS:SAAS00056878};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01169};
GN   Name=odhA {ECO:0000256|HAMAP-Rule:MF_01169};
GN   ORFNames=AZI98_18445 {ECO:0000313|EMBL:KZN94681.1};
OS   Aeribacillus pallidus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Aeribacillus.
OX   NCBI_TaxID=33936 {ECO:0000313|EMBL:KZN94681.1, ECO:0000313|Proteomes:UP000076476};
RN   [1] {ECO:0000313|EMBL:KZN94681.1, ECO:0000313|Proteomes:UP000076476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8m3 {ECO:0000313|EMBL:KZN94681.1,
RC   ECO:0000313|Proteomes:UP000076476};
RA   Poltaraus A.B., Nazina T.N., Tourova T.P., Malakho S.M.,
RA   Korshunova A.V., Sokolova D.S.;
RT   "Draft genome sequence of Aeribacillus pallidus 8m3 from petroleum
RT   reservoir.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-
CC       oxoglutarate dehydrogenase (E1), dihydrolipoamide
CC       succinyltransferase (E2) and lipoamide dehydrogenase (E3).
CC       {ECO:0000256|HAMAP-Rule:MF_01169, ECO:0000256|SAAS:SAAS00056852}.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC       {ECO:0000256|HAMAP-Rule:MF_01169, ECO:0000256|SAAS:SAAS00010311}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01169,
CC         ECO:0000256|SAAS:SAAS00342182};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01169,
CC       ECO:0000256|SAAS:SAAS00010313}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01169,
CC       ECO:0000256|SAAS:SAAS00538899}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KZN94681.1}.
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DR   EMBL; LWBR01000079; KZN94681.1; -; Genomic_DNA.
DR   RefSeq; WP_063389707.1; NZ_LWBR01000079.1.
DR   EnsemblBacteria; KZN94681; KZN94681; AZI98_18445.
DR   Proteomes; UP000076476; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
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; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 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; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076476};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01169,
KW   ECO:0000256|SAAS:SAAS00010314};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01169,
KW   ECO:0000256|SAAS:SAAS00010307};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076476};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01169,
KW   ECO:0000256|SAAS:SAAS00010309}.
FT   DOMAIN      599    795       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   947 AA;  107744 MW;  32744731ECE8AD7C CRC64;
     MEETSSNLKI AWRDFHGPNL GYVMDLYEQY LEDPNSVDEE LRNMFDAWGA PEALTEQSYV
     NSSSTVSRNL SYTFEKLQKV AAAVRFAEDI RTFGHLDASI YPMGIKHNEE DVLNESRYGL
     TKEDLIEIPA KLLSPYTPDH VHNGYEAIQY LKDVYSKSIA FEFQHVHNFE EHEWLNEMVE
     SGKIFKTLSK EKRISLLKRL TEVEGFESFL HKTFVGQKRF SIEGVDMLVP MLDELISEAV
     KSGTTNINIG MAHRGRLSVL AHVLGKPFEL IFSEFQHAPN KELVPSEGSI GINYGWTGDV
     KYHLGADRKI KDHNVVRARL TLANNPSHLE FVDPIVEGYT RAAQDNRNVR GYPEQDIHKS
     MAVLIHGDAA FPGEGVVAET LNLSQLNGYK TGGTIHIIAN NMIGFTTESH DSRSTKYASD
     LAKGFEIPIV HVNADDPEAC LAAVYIAILY RNKFHKDFLI DLIGYRRYGH NEMDEPMATN
     PLLYEKIKKH ETICKLYAKQ LESDGIISLE DARKFEQEVQ DRLKKAYDKV PKNEHQEEEI
     HIPETVSHGL PKIDTTVPVD VLDKINKELI TFPEGFTVFN KLQKILERRA KVYEEERKVD
     WSLAEAFAFA TILRDGTPLR ITGQDSERGT FAHRHLVLHD VKTGKTFSPL HRLSDVQASF
     AIHNSPLSEV SVLGFEYGYN VFSPETLVIW EAQFGDFANV AQVIFDQFIS AGRAKWGQKS
     GLVMLLPHGY EGQGPEHSSG RLERYLTLAA ENNWTVANVT TAAQYFHLLR RQAAILTKEE
     VRPLIIMTPK SLLRNPNTVS DVTELTEGQF QPVIEQPGLG QNKEKVKRLI LCTGKISIEL
     ANGLQKLDQK DFLHIVRVEE IYPFPEEEIK EIIERYPNLQ EIVWVQEEPK NMGSWIFTYP
     QLKSIVGDKL AVKYIGRPRR SSPAEGDPTI HKKEQSRIIT EALTWNE
//
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