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Database: UniProt
Entry: A0A1V3JNV9_9PAST
LinkDB: A0A1V3JNV9_9PAST
Original site: A0A1V3JNV9_9PAST 
ID   A0A1V3JNV9_9PAST        Unreviewed;       632 AA.
AC   A0A1V3JNV9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   31-JUL-2019, 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   Name=aceF {ECO:0000313|EMBL:OOF58506.1};
GN   ORFNames=BKL49_07060 {ECO:0000313|EMBL:OOF58506.1};
OS   Rodentibacter myodis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Rodentibacter.
OX   NCBI_TaxID=1907939 {ECO:0000313|EMBL:OOF58506.1, ECO:0000313|Proteomes:UP000188602};
RN   [1] {ECO:0000313|EMBL:OOF58506.1, ECO:0000313|Proteomes:UP000188602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac151 {ECO:0000313|EMBL:OOF58506.1,
RC   ECO:0000313|Proteomes:UP000188602};
RA   Christensen H.;
RT   "Rodentibacter gen. nov. and new species.";
RL   Submitted (OCT-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 3 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {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:OOF58506.1}.
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DR   EMBL; MLHQ01000016; OOF58506.1; -; Genomic_DNA.
DR   Proteomes; UP000188602; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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; IPR006256; AcTrfase_Pyrv_DH_cplx.
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:SF2; PTHR43178:SF2; 4.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 3.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 3.
DR   TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR   PROSITE; PS00189; LIPOYL; 3.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000188602};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:OOF58506.1};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:OOF58506.1}.
FT   DOMAIN        2     75       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      101    174       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      200    273       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      323    360       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      285    307       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   632 AA;  65910 MW;  9FAB2DED9BD8A4B0 CRC64;
     MSKQIQIPDI GSDEVTVTEV MVKVGDTVSV DQSIINVEGD KASMEVPAPE AGVVKEVLVK
     VGDKVTTGTP MLVLDSAEAA APAQAEVQAA PAATAPAAAS IVEVNVPDIG SDEVNVTEIM
     VKVGDAVEVD QSIINVEGDK ASMEVPAPIA GVVKEILINV GDKVSTGKLI MKFEVAGASP
     AASAPAQESA PAAAPSVAAI KDVNVPDIGG DEVNVTEIMV AVGDTVSEEQ SLITVEGDKA
     SMEVPAPFAG VVKEILVKSG DKVSTGSLIM RFEVASAAPA APVTQTAAPA PKAESAPTAQ
     ASQSGNVSGL SQEQVVASAG YAHATPVIRR LAREFGVNLD KVKGTGRKGR IVKEDIEAYV
     KTAVKAYESG ATAAAAGNGV ANGAGLGLLP WPKVDFSKFG EVEEVELSRI NKISGANLHR
     NWVMIPHVTH FDKADITDLE AFRKEQNALA EKQKLGVKIT PVVFIMKAVA KALEAFPRFN
     SSLSEDAQRL ILKKYINIGV AVDTPNGLVV PVFKNVNKKG IIELSRELME VSKKAREGKL
     TASDMQGGCF TISSIGGLGT THFAPIVNAP EVAILGVSKS AMEPVWNGKE FAPRLILPIS
     LSFDHRVIDG ADGARFISYI GSVLADLRRL IM
//
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