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Database: UniProt
Entry: A0A1G7XVA7_9SPHI
LinkDB: A0A1G7XVA7_9SPHI
Original site: A0A1G7XVA7_9SPHI 
ID   A0A1G7XVA7_9SPHI        Unreviewed;       552 AA.
AC   A0A1G7XVA7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 12.
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=SAMN05192573_105181 {ECO:0000313|EMBL:SDG87983.1};
OS   Mucilaginibacter gossypii.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=551996 {ECO:0000313|EMBL:SDG87983.1, ECO:0000313|Proteomes:UP000199705};
RN   [1] {ECO:0000313|EMBL:SDG87983.1, ECO:0000313|Proteomes:UP000199705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gh-67 {ECO:0000313|EMBL:SDG87983.1,
RC   ECO:0000313|Proteomes:UP000199705};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; FNCG01000005; SDG87983.1; -; Genomic_DNA.
DR   Proteomes; UP000199705; Unassembled WGS sequence.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; 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; 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   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   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:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199705};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:SDG87983.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199705};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:SDG87983.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      128    203       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      254    291       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       95    119       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1G7XVA7}.
FT   REGION      212    256       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1G7XVA7}.
SQ   SEQUENCE   552 AA;  57781 MW;  27EDCB337D8FA2CE CRC64;
     MAEVVKMPKM SDTMTEGVLA KWHKKVGDKV KSGDVLAEIE TDKATMDFES YQDGTLLYIG
     IQEGAAAPVD SVIAILGKEG EDYKSLLDQA GSGAAAEPAK EAAPAADRAP AATPAPAAPK
     VDLSSIPATV IRMPLLSDTM TEGTIEKWNF KVGDKVKADD SLADVATDKA TMEVVGYEAG
     TLLYIGVKEG EAAKVNDIIA IVGKEGTDIT PLLQDGGSAP AAEAAPGAEA KTEASASATA
     TAPESSSDDD SRVKASPLAR KIAKDKGINL NDVKGSAEGG RIIKKDVEEY TPSAKPAAAP
     VTEAAPAAAP AAAAKAPIVL PTFTGEEKFS ERPVTQMRKA ISRRLSESLF TAPHFYVTMS
     IDMDQAIVAR TRMNEIAPVK ISFNDFVVKA CAVALRQHPA INSSFLGDKI RTNEHVHVGV
     AVAVDEGLLV PVIKFADGKS LSHISVEVKE FAGKAKSKKL QPNEMEGSTF TISNLGMFGV
     DEFTAIINTP NACILAVSGI QAVPVVKNGA VVPGNIMKVT LSADHRVVDG ATAAAFLQTL
     KQLLEEPVRL LI
//
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