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Database: UniProt
Entry: I0JJY3_HALH3
LinkDB: I0JJY3_HALH3
Original site: I0JJY3_HALH3 
ID   I0JJY3_HALH3            Unreviewed;       957 AA.
AC   I0JJY3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-SEP-2017, entry version 40.
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=kgd {ECO:0000313|EMBL:CCG44452.1};
GN   Synonyms=odhA {ECO:0000256|HAMAP-Rule:MF_01169};
GN   OrderedLocusNames=HBHAL_2096 {ECO:0000313|EMBL:CCG44452.1};
OS   Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 /
OS   NBRC 102448/ NCIMB 2269) (Sporosarcina halophila).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG44452.1, ECO:0000313|Proteomes:UP000007397};
RN   [1] {ECO:0000313|EMBL:CCG44452.1, ECO:0000313|Proteomes:UP000007397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / NBRC 102448/ NCIMB 2269
RC   {ECO:0000313|Proteomes:UP000007397};
RX   PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA   Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA   Oesterhelt D.;
RT   "Chloride and organic osmolytes: a hybrid strategy to cope with
RT   elevated salinities by the moderately halophilic, chloride-dependent
RT   bacterium Halobacillus halophilus.";
RL   Environ. Microbiol. 15:1619-1633(2013).
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}.
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DR   EMBL; HE717023; CCG44452.1; -; Genomic_DNA.
DR   ProteinModelPortal; I0JJY3; -.
DR   EnsemblBacteria; CCG44452; CCG44452; HBHAL_2096.
DR   KEGG; hhd:HBHAL_2096; -.
DR   PATRIC; fig|866895.3.peg.1105; -.
DR   KO; K00164; -.
DR   OrthoDB; POG091H03SK; -.
DR   Proteomes; UP000007397; Chromosome.
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:UP000007397};
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, ECO:0000313|EMBL:CCG44452.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007397};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01169,
KW   ECO:0000256|SAAS:SAAS00010309}.
FT   DOMAIN      595    791       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   957 AA;  108269 MW;  34DD1B6C9BACF647 CRC64;
     MSNLGSNERF WENFHGPNMG YVEEQYELYE EDPEAVDPSL KEVFDEHGAP EWMKEGDTQN
     TSASHTSEVD IAKVTSALKL VEAIRRHGHL QANIYSVGSD ERPSTNLLDI ETYGLTEKDL
     ENIPAKWVWP DSPLRLDNAL QVVKTLKEKY AGTTSFEFGH VNNEEERKWL LDKVDTGSFH
     VSFSNEEKKQ LLRRLAQVEG FENFLAKTFV AQKRFSIEGL DVMVPMLDHM IQSASNDKIK
     NIMMGMAHRG RLNVLAHTLG KPYDRIFSEF HHSPDKELIP SEGSTGINYG WTGDVKYHFG
     ARREVGNGEQ SATRVTLSHN PSHLEYVNPV VEGFTRAAQD DRSNPGYAEM DEDEAFGVLI
     HGDAAFIGEG VVAETLNMSD LPGYRTGGTL HIIANNLVGF TTNREKGRST RYASDLAKGF
     EIPIVHVNAD DPLACMSAMA FAYEYRQTFH KDILIDLVGY RRFGHNEMDE PRATQPRLYS
     EIDEHPTVAA IYEEQLRKDS VVEEGTLNDM KNEIENEMRN VYNNMSEHET TTPDVKERPS
     GVERTLDEIE TAVDIDRLRS LNEGMLERPE GFNGFKKLEK ILQRRSKMLE DGQKVDWATA
     EALAFASILE DGRPIRITGQ DTERGTFAHR HMVLHDVETG ETYCPLHGLE QANASFDIHN
     SPLSEAGVLG FEYGYSVQAP ETLVLWEAQF GDFANAGQVI FDQFVAAGRA KWGEQSNMVF
     LLPHGYEGQG PEHSSARLER FLQLAAENNW TVGNVTSSAQ YFHLLRRQAA ISTEEEERPL
     VLMTPKSLLR NQRVAVEGKY FSEGKFQPIM RQPGLTKEDD KAKEKVKTLL LGSGKIMVDI
     EDTVEKAEDH SFETIDAVRI EQIYPFPKQR LKEILETYPN LEELVWVQEE PQNMGSWYFV
     EGILHKLLTG SQIHRYVGRP PRASPSVGEP NIHKTEQNRI IHEALQMSKG GKSNEGN
//
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