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Database: UniProt
Entry: H3NHS0_9LACT
LinkDB: H3NHS0_9LACT
Original site: H3NHS0_9LACT 
ID   H3NHS0_9LACT            Unreviewed;       571 AA.
AC   H3NHS0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=HMPREF9708_00348 {ECO:0000313|EMBL:EHR37719.1};
OS   Facklamia languida CCUG 37842.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR37719.1, ECO:0000313|Proteomes:UP000006190};
RN   [1] {ECO:0000313|EMBL:EHR37719.1, ECO:0000313|Proteomes:UP000006190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR37719.1,
RC   ECO:0000313|Proteomes:UP000006190};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia languida CCUG 37842.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHR37719.1}.
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DR   EMBL; AGEG01000003; EHR37719.1; -; Genomic_DNA.
DR   RefSeq; WP_006308291.1; NZ_JH601133.1.
DR   AlphaFoldDB; H3NHS0; -.
DR   STRING; 883113.HMPREF9708_00348; -.
DR   PATRIC; fig|883113.3.peg.352; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_9; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000006190; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
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; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006190};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EHR37719.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          113..188
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          251..288
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          76..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  60847 MW;  83E5D19919ED72DC CRC64;
     MAFQFKLPAL GEGIMEGEIV SWAVKEGDTI EEDQTLVEVQ NDKSVEELPS PVAGTITKIL
     VQEGTVAHLG EPLVEIDAPG HEDNSEEAAP AQAEEAEAAP AASQPAASGS TAYFQFKLPA
     LGEGIMEGEI VSWAVNEGDT IEEDNTIVEV QNDKSVEELP SPVSGVVKKI HVPAGQIAQL
     GDVLVEIDSP DHNGQAGDAE AAQAHANAYD DAAAPAEEVP ADPRGESQKQ DTSIEVSQGL
     SDEEAKNRRV LAMPSVRKLA RDKGFDITRI PGSGKNGRIT REDVENFNPA ANAGQSAAQQ
     PAAPAGQEQA QAAGVEQSAA PASQPAAPAK PFTSSQAERE ERVAMSGTRT AIAQAMVNSK
     HTAPHVTLYD EVEVSKLWAH RKKYKEVAAE QDVKLTFLPY VVKALIAAAK KYPVINASID
     DVSNEIVYKN YYNIGIATDT DRGLYVPNIK NANTKNMFQI AQEIVDLSSK AHDGSLQMSE
     MSEGTITISN IGSAGGKWFS PIINHPEVAI LGFGSIVQQP IVNEEGELAV GRVCKLSLSF
     DHRIVDGATA QRALNEVKRF LADPELLLME G
//
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