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Database: UniProt
Entry: A0A1M3HKP3_9SPHI
LinkDB: A0A1M3HKP3_9SPHI
Original site: A0A1M3HKP3_9SPHI 
ID   A0A1M3HKP3_9SPHI        Unreviewed;       553 AA.
AC   A0A1M3HKP3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   31-JUL-2019, entry version 14.
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=BGO55_20255 {ECO:0000313|EMBL:OJW59029.1};
OS   Sphingobacteriales bacterium 50-39.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW59029.1, ECO:0000313|Proteomes:UP000184242};
RN   [1] {ECO:0000313|EMBL:OJW59029.1, ECO:0000313|Proteomes:UP000184242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=50-39 {ECO:0000313|EMBL:OJW59029.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T.,
RA   Anantharaman K., Tringe S., Hettich R.L., Harrison S.T.,
RA   Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process
RT   performance in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA =
CC         (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={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}.
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:OJW59029.1}.
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DR   EMBL; MKTZ01000008; OJW59029.1; -; Genomic_DNA.
DR   Proteomes; UP000184242; Unassembled WGS sequence.
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; 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; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
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.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000184242};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:OJW59029.1};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:OJW59029.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      131    206       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      266    303       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       87    123       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      224    255       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   553 AA;  57623 MW;  775D9AFF19048248 CRC64;
     MAEVILMPRL SDTMTEGVIA SWHKKVGDTV KKGDLLAEVE TDKATMDLES YKDGTLLYVG
     TDKGGKVQVN ELLAIIGAPG EDISSLLKGG GAPAATSAPA DQQKATSPAP ASAPAATAAP
     AAQGEDISKL EGVILMPRLS DTMTEGVIAD WHKKVGDTVK KGEILADIET DKATMELESY
     KDGKLLHIGA QKGEKIAVND LLAVIGDESK VDLSRILAGA RNKGVPGPVA AGGTQPATSA
     QASAPAANGA APATGTLSVT ADGRIKASPL AKKIAAEKGI DISQVTGSGD NGRITKKDID
     NFVPGKPAAP ASQPAAKGAI PAAPAGQVSF EDVPVSQMRK VIAKRLSESK FTAPHFYVTM
     AIDMDKAIES RTKLNEVSPV KISFNDLVLK AVATALKQHP AINSSWLGDK IRINHHVNIG
     VAVAIEDGLV VPVVRFADTK TLSQIAAEVK DLAQRAKARK LQPADWEGST FTISNMGMFG
     VDEFTAIINT PDACILAVSA IQQVPVVKNG AVVPGNIMKL TLSCDHRVVD GAIGSAFLQT
     VKSLLEEPLR MML
//
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