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Database: UniProt/TrEMBL
Entry: A0A0H4VIK7_9BACT
LinkDB: A0A0H4VIK7_9BACT
Original site: A0A0H4VIK7_9BACT 
ID   A0A0H4VIK7_9BACT        Unreviewed;       572 AA.
AC   A0A0H4VIK7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   ORFNames=TH63_05605 {ECO:0000313|EMBL:AKQ45228.1};
OS   Rufibacter sp. DG31D.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=1379910 {ECO:0000313|EMBL:AKQ45228.1, ECO:0000313|Proteomes:UP000036458};
RN   [1] {ECO:0000313|EMBL:AKQ45228.1, ECO:0000313|Proteomes:UP000036458}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG31D {ECO:0000313|EMBL:AKQ45228.1,
RC   ECO:0000313|Proteomes:UP000036458};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Rufibacter sp./DG31D/ whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP010777; AKQ45228.1; -; Genomic_DNA.
DR   RefSeq; WP_048920086.1; NZ_CP010777.1.
DR   EnsemblBacteria; AKQ45228; AKQ45228; TH63_05605.
DR   KEGG; ruf:TH63_05605; -.
DR   PATRIC; fig|1379910.4.peg.1223; -.
DR   KO; K00627; -.
DR   Proteomes; UP000036458; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate 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; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR006257; LAT1.
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   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036458};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:AKQ45228.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036458};
KW   Transferase {ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      135    210       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   572 AA;  59619 MW;  EAA17D7880A0B708 CRC64;
     MAEIIRMPKM SDTMTEGVIA SWLKKVGDSV KSGDVLAEVE TDKATMELES YEDGTLLYIG
     PKNGESVPVD GVLAIIGKEG EDISGLMAEA GGSAPAPAQA EAPKKEEAPA AEPKKEEPAQ
     EAAPAAQPAA ANVKAEVVRM PKMSDTMQEG TIVAWHKKVG DKVKSGDLLA EVETDKATME
     LESYEDGTLL YIGVEAGASV QVDGILAIIG EEGADYKALL NGGGNTNPAQ AGSQEQATRV
     EEHKTEAQSQ SGDGVNQAAG APVPGQGTAP AAAGENQGRV LASPLAKKVA QEKGVSLSQI
     KGSGENGRIV LRDVENFTPS AAAAPKAQAP QAAAPAAPAA APAQAGEAFT EVPVTQMRKV
     IARRLAESLF TAPHFYLTME IDMDKAMEAR VVMNEVAPVK VSFNDMVIKA AAAALRKHPA
     VNSSWLGDKI RYNNVVNIGV AVAVEDGLLV PVVRNADQKS LSTISAEVKD LGGKAKTKKL
     QPSDWEGSTF TISNLGMFGI DEFTAIINPP DACILAVGGI KQTPVVKNGQ IQIGNVMKVT
     LSCDHRVVDG AVGSAFLQTL KGFLENPVTM LV
//
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