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Database: UniProt
Entry: A0A1M5H6L4_9ALTE
LinkDB: A0A1M5H6L4_9ALTE
Original site: A0A1M5H6L4_9ALTE 
ID   A0A1M5H6L4_9ALTE        Unreviewed;       660 AA.
AC   A0A1M5H6L4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   05-JUN-2019, entry version 12.
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=SAMN05216361_1336 {ECO:0000313|EMBL:SHG11681.1};
OS   Aestuariibacter aggregatus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Aestuariibacter.
OX   NCBI_TaxID=634436 {ECO:0000313|EMBL:SHG11681.1, ECO:0000313|Proteomes:UP000184520};
RN   [1] {ECO:0000313|EMBL:SHG11681.1, ECO:0000313|Proteomes:UP000184520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8995 {ECO:0000313|EMBL:SHG11681.1,
RC   ECO:0000313|Proteomes:UP000184520};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQWD01000002; SHG11681.1; -; Genomic_DNA.
DR   RefSeq; WP_073319731.1; NZ_FQWD01000002.1.
DR   BioCyc; GCF_900129565:BUB81_RS05895-MONOMER; -.
DR   Proteomes; UP000184520; 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:UP000184520};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:SHG11681.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184520};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:SHG11681.1}.
FT   DOMAIN        4     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      120    196       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      228    304       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      356    393       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       87    120       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1M5H6L4}.
FT   REGION      312    360       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1M5H6L4}.
FT   COMPBIAS    316    345       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A1M5H6L4}.
SQ   SEQUENCE   660 AA;  68398 MW;  24DE0184D27FEE21 CRC64;
     MSDIKDVFVP DLGEDEVEVI ELCVSPGDSV EAEDALVTVE SDKASMDVPA PFAGTVKELC
     VNVGDKIKQS DLLAKLEVAG AGAAPAASEP EAPAAPAAAE PAAPAAAAEP APAPAASGAS
     QTIEVTVPDI GDAADVDVIE ILVSVGDEVQ AEDGLITLET DKATMDVPCP QAGKVVELKV
     KEGDKVSEGS LVLLLEVGGA AEASAPAAEA APAPAAAPAA EASAPAADEE IEVTVPDIGD
     ASDVDVIEVL VSEGDTVAIE DGLITLETDK ATMDVPSPKA GVVTKLLVNT GDKVSKGSKV
     CILKVQGAAK PAAPAPQPAA SAPAPAAKAP EPGKPKPPPV PHHPSAGNKP KTGKVHASPS
     VRRLAREFGV DLAEVSGSGP KNRILKEDIQ SYVKYELSRP KATPGAVASG NGGLQVLAQP
     KVDFSKFGEI EEKPLTRIQK ISGPNLHRNW VTIPHVTQFE EADITDLEAF RKEQNAIAEK
     RKLGVKITPL VFMMKAAADA LRAYPIFNTS LGESGETLIQ KKYIHIGLAV DTPGGLVVPV
     VRDVDKKGIY ELSEELMEIS KKARDGKLKA ADMQGSCFTI SSLGGIGGTG FTPIVNAPDV
     AILGVSKSDI KPKWNGKEFE PRLTVPLSLS YDHRVIDGAV AARFAVHLKN VLEDLRQLIL
//
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