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Database: UniProt
Entry: A0A221W2Q8_9PSEU
LinkDB: A0A221W2Q8_9PSEU
Original site: A0A221W2Q8_9PSEU 
ID   A0A221W2Q8_9PSEU        Unreviewed;       441 AA.
AC   A0A221W2Q8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   05-JUN-2019, entry version 9.
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=pdhC1 {ECO:0000313|EMBL:ASO19891.1};
GN   ORFNames=AHOG_11240 {ECO:0000313|EMBL:ASO19891.1};
OS   Actinoalloteichus hoggarensis.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinoalloteichus.
OX   NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO19891.1, ECO:0000313|Proteomes:UP000204221};
RN   [1] {ECO:0000313|EMBL:ASO19891.1, ECO:0000313|Proteomes:UP000204221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO19891.1,
RC   ECO:0000313|Proteomes:UP000204221};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943,
RT   type strain of Actinoalloteichus hoggarensis.";
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 1 lipoyl cofactor covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP022521; ASO19891.1; -; Genomic_DNA.
DR   KEGG; ahg:AHOG_11240; -.
DR   KO; K00627; -.
DR   Proteomes; UP000204221; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
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; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 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:RU361137,
KW   ECO:0000313|EMBL:ASO19891.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000204221};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:ASO19891.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204221};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ASO19891.1}.
FT   DOMAIN        1     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      137    174       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       77    141       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A221W2Q8}.
FT   REGION      179    208       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A221W2Q8}.
SQ   SEQUENCE   441 AA;  45737 MW;  0AF390C2ABFF670F CRC64;
     MTEIQMPRLS DTMEEGVISA WVKQEGDTIS RGDVVAEIET DKAVMELEAY DDGVLEKILV
     PAGELVPIGA TIGLLGDGSG SASAAPAAPS TTAPEGTGAA ESAAAAESTD QTEAPADVSS
     AAPRVDQAPT PAGSRPRSSP LARKIAREAG IDLDTVAGSG PRGRIVRADV DAAVAAKQSA
     DAAAPAQQAE PTETAAPSAP RTGIAADTED VEEIPLSGIR RVAAKRLTES KQQAPHFYLT
     SAVDVTELLG FRADLTAKVQ AAGGPKVSIN DLLVKAVATA LRANPTVNVS FAGDKILQHK
     RIHLGIAVAI ESGLVVPVLR DADRKSVSEL ASEAREKAGR AREGRLKTDE MTGGTFTISN
     LGMFGIEEFA AVINPPEAAI LAVGAVRDEL RLRAEGKNKV EVRKIMRITL SADHRAVDGA
     VGAVFLQQLT ALLEDPIRII A
//
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