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Database: UniProt
Entry: B2UQI3_AKKM8
LinkDB: B2UQI3_AKKM8
Original site: B2UQI3_AKKM8 
ID   B2UQI3_AKKM8            Unreviewed;       424 AA.
AC   B2UQI3;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Amuc_0885 {ECO:0000313|EMBL:ACD04718.1};
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD04718.1, ECO:0000313|Proteomes:UP000001031};
RN   [1] {ECO:0000313|Proteomes:UP000001031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC   / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CP001071; ACD04718.1; -; Genomic_DNA.
DR   RefSeq; WP_012419933.1; NC_010655.1.
DR   AlphaFoldDB; B2UQI3; -.
DR   STRING; 349741.Amuc_0885; -.
DR   PaxDb; 349741-Amuc_0885; -.
DR   KEGG; amu:Amuc_0885; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_0; -.
DR   OMA; HSRVNKP; -.
DR   BioCyc; AMUC349741:G1GBX-957-MONOMER; -.
DR   Proteomes; UP000001031; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 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   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001031};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          160..200
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          82..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  45378 MW;  11F941641A74F77D CRC64;
     MPKVPILMPQ LGDSIAEATV LRLLAAQGDT VEADQEIFEV ETNKATMGVT TMCGGILSDV
     FIKEGESVVV GACMAMIEAT EEEIERSGAT PAGDSTQPSL PASPESVPQA APSAPPREEK
     PAGVHFGVTG ESYQENGTDL KVQPSVRGLP VPAGMKGAHY MSPRMKARMD ELGMSASDIA
     FISGSGAGGR VTIDDLEEFL EYVSQWPHRK ASSMRLAVAD AMRRSWTRPL ASAGRPVFMD
     PLIKHRQNSP LRPGITLYFA RALALSLAES PECAGYLVGE NILSPKTIDI GIAAQVADGV
     MVPVLRRVNE RTMEELLEDY NRLIAQARRR RLAPEDSTGG IATVTNFGGF GLTFAAPMPM
     PSESIILGVG AVTKTPVWSD EVEAFIPISK ANIVATGDHR VVDGADIGRL LKRVAELLQR
     PEYL
//
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