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Database: UniProt
Entry: A0A1I6D4Y5_9FIRM
LinkDB: A0A1I6D4Y5_9FIRM
Original site: A0A1I6D4Y5_9FIRM 
ID   A0A1I6D4Y5_9FIRM        Unreviewed;       530 AA.
AC   A0A1I6D4Y5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 11.
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=SAMN05660706_10586 {ECO:0000313|EMBL:SFR00362.1};
OS   Desulfallas geothermicus DSM 3669.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfallas.
OX   NCBI_TaxID=1121426 {ECO:0000313|EMBL:SFR00362.1, ECO:0000313|Proteomes:UP000199584};
RN   [1] {ECO:0000313|EMBL:SFR00362.1, ECO:0000313|Proteomes:UP000199584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3669 {ECO:0000313|EMBL:SFR00362.1,
RC   ECO:0000313|Proteomes:UP000199584};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity.
CC       Required for the reduction of the AhpC active site cysteine
CC       residues and for the regeneration of the AhpC enzyme activity.
CC       {ECO:0000256|SAAS:SAAS00088543}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide
CC         + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593,
CC         Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC         EC=1.11.1.15; Evidence={ECO:0000256|SAAS:SAAS01192926};
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   -!- SIMILARITY: Belongs to the AhpD family.
CC       {ECO:0000256|SAAS:SAAS00571262}.
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DR   EMBL; FOYM01000005; SFR00362.1; -; Genomic_DNA.
DR   BioCyc; GCF_900115975:BM299_RS04440-MONOMER; -.
DR   Proteomes; UP000199584; Unassembled WGS sequence.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1290.10; -; 1.
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; IPR029032; AhpD-like.
DR   InterPro; IPR004675; AhpD_core.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR003779; CMD-like.
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; 1.
DR   Pfam; PF02627; CMD; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF69118; SSF69118; 1.
DR   TIGRFAMs; TIGR00778; ahpD_dom; 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:RU003423};
KW   Antioxidant {ECO:0000256|SAAS:SAAS00461132};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199584};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00461175};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00461144};
KW   Peroxidase {ECO:0000256|SAAS:SAAS00461184};
KW   Pyruvate {ECO:0000313|EMBL:SFR00362.1};
KW   Redox-active center {ECO:0000256|SAAS:SAAS00461089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199584};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:SFR00362.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      128    165       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   COILED      282    309       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   530 AA;  57103 MW;  2E0AEA39404DB832 CRC64;
     MANIVLMPKL GLTMKKGRIY GWLKNEGDRV ELGEPLLEVM TEKVNIKVES PFAGVLYKIL
     CAKGTTLPIS TPIAVMAEAG DDEAALEAAV SKARAALEEA LAGAGKEEGR KKEVKAVKPF
     VVFTGDRKVS PRAAKLARKE GVDIGLISGS GPGGRVVEED VRAYLEQLQG NESCQTMPID
     GMRAVIAERM SGSRKQAAHV TVMEEVDVTA LRDVRSQLNA LDDSGKIKFS YTDLLVKFVA
     EALTEYQMVN SCSSESEIIL PSSVNIGVAV ALENGLVVPN IKNAQRLNLE QISAKVKDLA
     ARARNNELDP EDIEGGTFTI SNLGMFGAEG FTPIINRPET AILGVGTMRA KPDLAGGKLV
     KRYFMTLSLS FDHRIIDGSL AAEFLSRLKE MLEDPHPWFG LQSQYSEELL ISAGGNKSPQ
     QIRKAYQNGI DKLMETAPDV VMGFSTLTEG IFFDDGAVSR LDKELIAVAL SVCIKCEYCI
     AAHVYKAMEL GATPEQVLEA ANVAVFFGGG AALAYTSTLV QDCIEAFGKN
//
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