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Database: UniProt/TrEMBL
Entry: A0A088ET49_9SPHI
LinkDB: A0A088ET49_9SPHI
Original site: A0A088ET49_9SPHI 
ID   A0A088ET49_9SPHI        Unreviewed;       542 AA.
AC   A0A088ET49;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   07-JUN-2017, entry version 16.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   ORFNames=KO02_02295 {ECO:0000313|EMBL:AIM35629.1};
OS   Sphingobacterium sp. ML3W.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1538644 {ECO:0000313|EMBL:AIM35629.1, ECO:0000313|Proteomes:UP000028992};
RN   [1] {ECO:0000313|EMBL:AIM35629.1, ECO:0000313|Proteomes:UP000028992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ML3W {ECO:0000313|EMBL:AIM35629.1};
RX   PubMed=25614576;
RA   Smith S.A., Krasucki S.P., McDowell J.V., Balke V.L.;
RT   "Complete Genome Sequence of Sphingobacterium sp. Strain ML3W,
RT   Isolated from Wings of Myotis lucifugus Infected with White Nose
RT   Syndrome.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CP009278; AIM35629.1; -; Genomic_DNA.
DR   RefSeq; WP_038695461.1; NZ_CP009278.1.
DR   EnsemblBacteria; AIM35629; AIM35629; KO02_02295.
DR   KEGG; sht:KO02_02295; -.
DR   KO; K00627; -.
DR   Proteomes; UP000028992; Chromosome.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
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; IPR004167; E3-bd.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028992};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:AIM35629.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028992};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      124    199       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   542 AA;  57443 MW;  B3D77F2350700A2E CRC64;
     MAEVVRMPKM SDTMTEGVIA KWHKQVGDKV NSGDLVAEIE TDKATMDFES YQEGTLLYIG
     PKEGEAVAID AIIAILGEPG EDFQSLLSDA PQVVAEVEKK EEVSTSSDTA IAPQSDVTPE
     SLGVTVITMP LLSDTMTEGV IAQWNFKVGD TIKSDDSIAD VETDKATMEV TAYADGTLLY
     VGLEAGEAAK VNDIIAIVGP AGTDVTPLLN QKTAVTQPAA TEVKEEAKVE SGGSVENKAS
     DVIDDSRVKA SPLARKIAKD KGINLNDVKG SADGGRIVKK DVESYAPAAK SAPVSAASTA
     VATETKAISL PSYVGEERYT EVAVSQMRKT IARRLGESLF TAPHFYLTVS IDMENAMLAR
     TQINEVAPVK VSFNDIVVKA VAVALKKHPA VNSSWKGDKI RFNEHTNIGV AMAVEDGLLV
     PVVRFADGKS LSHISAEVKD FAQKAKTKKL TPADWEGSTF TVSNLGMFGI DEFTSIINSP
     DGAILSVGAI QQVPVVKNGA VVPGNVMKLT LGCDHRVVDG ANGAQFLQTL KALLENPVRL
     LA
//
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