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Database: UniProt
Entry: A0A2A2I467_9ALTE
LinkDB: A0A2A2I467_9ALTE
Original site: A0A2A2I467_9ALTE 
ID   A0A2A2I467_9ALTE        Unreviewed;       551 AA.
AC   A0A2A2I467;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-JUN-2019, entry version 8.
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:PAV26519.1};
GN   ORFNames=CF392_04745 {ECO:0000313|EMBL:PAV26519.1};
OS   Tamilnaduibacter salinus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Tamilnaduibacter.
OX   NCBI_TaxID=1484056 {ECO:0000313|EMBL:PAV26519.1, ECO:0000313|Proteomes:UP000218332};
RN   [1] {ECO:0000313|EMBL:PAV26519.1, ECO:0000313|Proteomes:UP000218332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mi-7 {ECO:0000313|EMBL:PAV26519.1,
RC   ECO:0000313|Proteomes:UP000218332};
RA   Verma A., Krishnamurthi S.;
RT   "Tamlnaduibacter salinus (Mi-7) genome sequencing.";
RL   Submitted (JUL-2017) 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   -!- 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:PAV26519.1}.
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DR   EMBL; NMPM01000020; PAV26519.1; -; Genomic_DNA.
DR   Proteomes; UP000218332; 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; 3.
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; TIGR01348; PDHac_trf_long; 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:UP000218332};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218332};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:PAV26519.1}.
FT   DOMAIN        3     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      122    196       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      253    290       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       25    132       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2A2I467}.
FT   REGION      167    255       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2A2I467}.
FT   COMPBIAS     83    109       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A2A2I467}.
FT   COMPBIAS    177    198       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A2A2I467}.
SQ   SEQUENCE   551 AA;  58340 MW;  A3BBD5E9005F9ECA CRC64;
     MSTQDIKVPD LGGADEVEII EITVSEGDQV EEEDPILTVE SDKASVELPA PASGTIQSLT
     VKVGDKLKEG DVVGTMEAGE SGGADDRASE DKDEASDTVS SDSESDEPKE SATPAPSGGT
     RQETVKVPNL DGFDNVPVIE INVSVGDEVE EEDALVSVES DKATMEIPSS HAGRIEEVLV
     NEGDKISEGD DLVRMTITEE GGEEAAAAEG PAKSSGKEEA PAEPGQDKAP SEPQPAAEPA
     SSEPVTKPGA AVHAGPAVRK LAREFGADLT RIKGSGPKGR VLKDDVQSYV KGQLKQTQEG
     GAAASAGGIP GIKLPDFSQF GEVQRESMTR MQVATAENMH RSWLNVPHVT QHDDADITDL
     EAFRKSQKAA GEKRGVKMTP MPFLLKAAAQ ALAELPQFNV SLDMERREIV RKQYIHIGIA
     VDTPSGLMVP VIRDVDKKGL WELAEEAGDL AAKARDKKLK PDEMKGACFS ITSLGGIGGT
     AFTPIVNPPE VAILGVSKAA MKPVWDGDAF QPRLMMPLSL SYDHRAVNGA DAARFTSLMG
     ELLGDIRRLL L
//
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