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Database: UniProt
Entry: A0A0M0X8U0_9BACI
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ID   A0A0M0X8U0_9BACI        Unreviewed;       946 AA.
AC   A0A0M0X8U0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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=AMS60_08930 {ECO:0000313|EMBL:KOP82587.1};
OS   Bacillus sp. FJAT-21945.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1581033 {ECO:0000313|EMBL:KOP82587.1, ECO:0000313|Proteomes:UP000036921};
RN   [1] {ECO:0000313|Proteomes:UP000036921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-21945 {ECO:0000313|Proteomes:UP000036921};
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   "Fjat-21945.";
RL   Submitted (AUG-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:KOP82587.1}.
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DR   EMBL; LITN01000002; KOP82587.1; -; Genomic_DNA.
DR   RefSeq; WP_053476136.1; NZ_LITN01000002.1.
DR   EnsemblBacteria; KOP82587; KOP82587; AMS60_08930.
DR   PATRIC; fig|1581033.3.peg.3065; -.
DR   Proteomes; UP000036921; 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:UP000036921};
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:UP000036921};
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   946 AA;  106535 MW;  A9FC9F5C48A120F0 CRC64;
     MKKPLNGEKP FAEGFHGPNL GYVIELYEAY LENPESVDPE MRAYFETTGS PVVENRTGKT
     EISGVNQTVP QLEKTLSAIR LADNIRTYGH LAANIYPLND HEPEKMLFEL SHYGLIEEDL
     YAIPAGVICK DAPIPLKNAY DAIEYLKSMY MGTIAFEFHH VYDANEKNWL RRKVESGSLK
     LKLQKEEKTK ILKRLTEVEE FEKFLHRTFV GQKRFSIEGL DSMVPLLDEI VAESVSKGAK
     TINIGMAHRG RLNVLAHVLG KPYEMIFAEF QHAPNKELVP SEGSIGISYG WTGDVKYHLG
     LDKQIKDENT TVTRLTLANN PSHLEFVGSV VEGFTRAAQD NRSTKGYPIE NLNSAMSIII
     HGDAAFPGQG IVAETLNLGQ LKGYNTGGSL HIIANNTIGF TTESRDSRST RYASDLAKGF
     EIPILHVNAD DPESCIAAAR FASEYREKFQ KDFLIDLIGY RRFGHNEMDE PMATNPLMYK
     IINEQPTVKE LYGKKLVNQL IINKDTADKI EEDVLVKLKA AYEKVPATKK ETEELNPPET
     VEKGLPKLKT AVPFEKLKEI NRELLTWPEK FTVFNKLDKI LNRRMSALDG EKKIDWGHAE
     TLAFASILHD GTPIRLTGQD SERGTFAHRN IVLHDSSTGK SYSPLHLLSS AKASFAVHNS
     PLSEAAVLGF EYGYNVFAPE TLVLWEAQFG DFANSAQVIF DQFIAAGRAK WGQKSGLVML
     LPHGYEGQGP EHSSARLERF LTLAAENNWT VANLTSAAQY FHILRRQAAI LKREEVRPLV
     IMAPKSLLRH PLVASSGHEL SEGDFQSVIE QPGLGQNTDK VTRLVLSTGK MAIDLADNLK
     NVDNQEWFHL LRVEEIYPFP LETIQTIMKR YPNLKEMVWV QEEPKNMGSW NFVEPRLQFI
     AQKEIDVSYI GRRRRSSPSE GDPNVHKKEQ ARIIEEAFMH KQEGGN
//
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