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Database: UniProt
Entry: A0A0Q3TIT0_9BACI
LinkDB: A0A0Q3TIT0_9BACI
Original site: A0A0Q3TIT0_9BACI 
ID   A0A0Q3TIT0_9BACI        Unreviewed;       940 AA.
AC   A0A0Q3TIT0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-2017, entry version 12.
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=AN964_10240 {ECO:0000313|EMBL:KQL53838.1};
OS   Bacillus shackletonii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL53838.1, ECO:0000313|Proteomes:UP000051888};
RN   [1] {ECO:0000313|EMBL:KQL53838.1, ECO:0000313|Proteomes:UP000051888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL53838.1,
RC   ECO:0000313|Proteomes:UP000051888};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-2015) 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:KQL53838.1}.
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DR   EMBL; LJJC01000004; KQL53838.1; -; Genomic_DNA.
DR   RefSeq; WP_055739575.1; NZ_LJJC01000004.1.
DR   EnsemblBacteria; KQL53838; KQL53838; AN964_10240.
DR   PATRIC; fig|157838.3.peg.2253; -.
DR   Proteomes; UP000051888; 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:UP000051888};
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:UP000051888};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01169,
KW   ECO:0000256|SAAS:SAAS00010309}.
FT   DOMAIN      594    790       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   940 AA;  105914 MW;  DCFA18A6158291C5 CRC64;
     MNDQASRGFW ESFSGPNLGY VMEVYEQYLN DPESVEPEMK ELFEQWGAPT VSNEVLSTSG
     QADVSFQMPT NATIFSKIVS AVKLADNIRT YGHLAADINP LNNTSKDTRR IELKEYNLTE
     EDLRQIPVSF ICPDAPSTVK NGLDAINYLK DVYTKKIAYE FHHVHNLEEK NWLQKTVESG
     KIYPQLSKEE KLNILKRLTE VEGFEKFAHR IFVGQKRFSI EGLDMMVPLM DKIISSSVEY
     GAKTVNIGMA HRGRLNVLAH ILEKPYELIF AEFQHAPNKD LIPSEGSIGI TYGWTGDVKY
     HLGADRVNKE SVRVVLANNP SHLEVAAPVV EGYTRAAQEN RKTSGYPEQN PEEALAIIVH
     GDAAFPGEGI VTETLNMSGL RGYNTGGSIH IISNNMIGFT TESFDSRSTK YSSDAAKGYE
     IPIIHVNADD PESCIAAAIF AAEYRRLFKK DFLIDLIGYR KFGHNETDEP MTTNPMMYQI
     VRKHPTVRTI YAEQLVNEGL LSKEDVQKLE ENVNAKLQAA YDKVPGADEN PDIVMNPPEY
     VASGYPAVKT SVDNEELKDL NAQLLNWPED FNVFKKLGKI LKRRENVFDG DGKIDWAHAE
     SLAFASILKD GTPIRMTGQD SQRGTFAQRN LVLHDEKTGE EYIPLHHLKD TNASFVVYNS
     PLTETAVLGF EYGYNVLSPE TLVLWEAQFG DFANMAQTMF DQFISAGRAK WGQKSGLVML
     LPHGYEGQGP EHSSARMERY LQMAAENNWT VANLSTAGQY FHILRRQAAM LGKDEIRPLV
     LMTPKSLLRH PLASVDSSEL TNSEFKPVLE QAGLGQNADK VERIVLCSGK IAIDLETRLQ
     EEENAEWLHI LRIEELYPFP ENQVKEILSR YKNLKEIVWV QEEPQNMGGW TFVDPYLRGL
     SPQGVDVKYA GRPRRSSPSE GDPVVHKKEQ NRIINEAFTK
//
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