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Database: UniProt
Entry: A0A0M2XMV8_9CORY
LinkDB: A0A0M2XMV8_9CORY
Original site: A0A0M2XMV8_9CORY 
ID   A0A0M2XMV8_9CORY        Unreviewed;       581 AA.
AC   A0A0M2XMV8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-JUN-2019, entry version 17.
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=WU86_00035 {ECO:0000313|EMBL:KKO82861.1};
OS   Corynebacterium xerosis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1725 {ECO:0000313|EMBL:KKO82861.1};
RN   [1] {ECO:0000313|EMBL:KKO82861.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 373 {ECO:0000313|EMBL:KKO82861.1};
RA   Pacheco L.G., Mattos-Guaraldi A.L., Santos C.S., Veras A.O.,
RA   Guimaraes L.C., Abreu V., Pereira F.L., Soares S.C., Dorella F.A.,
RA   Carvalho A.F., Leal C.G., Figueiredo H.C., Ramos J.N., Vieira V.,
RA   Farfour E., Guiso N., Hirata R.Jr., Ramos R.T., Azevedo V., Silva A.;
RT   "Draft Genome Sequences of Three Species of Emerging Human-Pathogenic
RT   Corynebacteria.";
RL   Submitted (APR-2015) 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}.
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:KKO82861.1}.
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DR   EMBL; LAYS01000001; KKO82861.1; -; Genomic_DNA.
DR   RefSeq; WP_046649408.1; NZ_LAYS01000001.1.
DR   EnsemblBacteria; KKO82861; KKO82861; WU86_00035.
DR   PATRIC; fig|1725.5.peg.8; -.
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; IPR014276; 2-oxoglutarate_DH_E2.
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   TIGRFAMs; TIGR02927; SucB_Actino; 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:RU003423};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:KKO82861.1};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      129    204       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      277    314       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       63    147       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0M2XMV8}.
FT   REGION      204    275       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0M2XMV8}.
FT   REGION      313    335       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0M2XMV8}.
FT   COMPBIAS     82    111       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A0M2XMV8}.
FT   COMPBIAS    112    126       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0M2XMV8}.
FT   COMPBIAS    209    223       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A0M2XMV8}.
FT   COMPBIAS    224    270       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0M2XMV8}.
SQ   SEQUENCE   581 AA;  62286 MW;  54A65D435F3AF446 CRC64;
     MATSVEMPEL GESVTEGTIT TWLKKVGDTV EVDEPLLEVS TDKVDTEIPS PVAGVLLEIL
     AEEDDTVDVG EVIAKIGDED ESGDSGSDDS ADEAEEDEAE EAAEDEAADD EKSEDKSEKP
     KKSGGSGKAS DVEMPELGES VTEGTITSWL KEVGDTVEVD EPLLEVSTDK VDTEIPSPVA
     GTLIEVLFDV DDTVDVGAVI ARVGDADAAD DGDDAEVEAA EAATEEKEEP KKKDQPKKAE
     PKKEEKKQEA KSEKSEPKKD DAKKDDAKSS SNAEVPYVTP LVRKLADKHG VDLSKVEGSG
     IGGRIRKQDV LKAAEGGTEA TKGDEPASSN WSTKGVRPEL ADLRGTTQRV NRIREITAAK
     TLESLQTSAQ LTQLHEVDMT EVWDLRAEKK AAFEEKHGVK LTFLPFFAKA MVEALVSHPN
     VNASWDDSKK EITYHEKVNL GIAVDTDRGL LSPVIHDAQD MSLPELAAAI VDIADRARNN
     KLKPNDLSGG TFTITNIGSE GALSDTPILV PPQGAMVGTG IIKKRAVVVT ENGSDAIGIR
     AMAYLPMTYD HRLIDGADAG RFMTTVVDRL QVANFESDLE L
//
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