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Database: UniProt
Entry: A0A0B8T793_9SPHI
LinkDB: A0A0B8T793_9SPHI
Original site: A0A0B8T793_9SPHI 
ID   A0A0B8T793_9SPHI        Unreviewed;       412 AA.
AC   A0A0B8T793;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUN-2019, entry version 27.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|RuleBase:RU361138};
DE            EC=2.3.1.61 {ECO:0000256|RuleBase:RU361138};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN   ORFNames=DI53_2621 {ECO:0000313|EMBL:KGE13560.1};
OS   Sphingobacterium deserti.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE13560.1, ECO:0000313|Proteomes:UP000031802};
RN   [1] {ECO:0000313|Proteomes:UP000031802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RA   Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C.,
RA   Zhang W.;
RT   "Whole-Genome optical mapping and complete genome sequence of
RT   Sphingobacterium deserti sp. nov., a new spaces isolated from desert
RT   in the west of China.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGE13560.1, ECO:0000313|Proteomes:UP000031802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RX   PubMed=25830331;
RA   Teng C., Zhou Z., Molnar I., Li X., Tang R., Chen M., Wang L., Su S.,
RA   Zhang W., Lin M.;
RT   "Whole-Genome Optical Mapping and Finished Genome Sequence of
RT   Sphingobacterium deserti sp. nov., a New Species Isolated from the
RT   Western Desert of China.";
RL   PLoS ONE 10:E0122254-E0122254(2015).
CC   -!- FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the second step in the conversion of 2-
CC       oxoglutarate to succinyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-
CC         (S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + CoA; Xref=Rhea:RHEA:15213,
CC         Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120;
CC         EC=2.3.1.61; Evidence={ECO:0000256|RuleBase:RU361138};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361138};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000256|RuleBase:RU361138};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC       saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361138}.
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:KGE13560.1}.
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DR   EMBL; JJMU01000048; KGE13560.1; -; Genomic_DNA.
DR   RefSeq; WP_037500123.1; NZ_JJMU01000048.1.
DR   STRING; 1229276.DI53_2621; -.
DR   EnsemblBacteria; KGE13560; KGE13560; DI53_2621.
DR   PATRIC; fig|1229276.3.peg.2693; -.
DR   OrthoDB; 1626282at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000031802; Unassembled WGS sequence.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031802};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031802};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:KGE13560.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      119    156       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       80    118       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B8T793}.
FT   REGION      136    186       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B8T793}.
FT   COMPBIAS     82     96       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0B8T793}.
FT   COMPBIAS    136    160       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0B8T793}.
SQ   SEQUENCE   412 AA;  44462 MW;  C9F04516EBCA97BF CRC64;
     MSLEIKVPAV GESITEVTLA QWLKQDGDYV EMDENIAELE SDKATFELPA EKAGILRIIA
     QEGDTLEIGA VVCSIEDGDA PAAGGAEKKE EAPAEKEQTP ASAPAKEDPE NPDSYAAGTA
     SPAAAKILRE KGIDASTIKG TGKEGRITKE DAEKAQAKPA APKAESKPAA TSSAPAVAGA
     RNERREKMTS LRKTIAKRLV SVKNETAMLT TFNEVNMQPI MDLRSKYKDT FKEKHGVGLG
     FMSFFTKAVT TALKEWPAVN ARIEENEIVF SDFADVSIAV SAPKGLVVPV IRNAESMSLY
     QIEKEIITLA TKARDNKLTI DEMTGGTFTI TNGGVFGSMM STPIINAPQS AILGMHNIVQ
     RPIAENGQVV IRPMMYIALS YDHRVIDGRE SVSFLVRVKQ LLEDPARLLL EV
//
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