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Database: UniProt
Entry: A0A1H1S483_9CELL
LinkDB: A0A1H1S483_9CELL
Original site: A0A1H1S483_9CELL 
ID   A0A1H1S483_9CELL        Unreviewed;       587 AA.
AC   A0A1H1S483;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-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=SAMN04489860_1531 {ECO:0000313|EMBL:SDS42900.1};
OS   Paraoerskovia marina.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Paraoerskovia.
OX   NCBI_TaxID=545619 {ECO:0000313|EMBL:SDS42900.1, ECO:0000313|Proteomes:UP000185663};
RN   [1] {ECO:0000313|EMBL:SDS42900.1, ECO:0000313|Proteomes:UP000185663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22126 {ECO:0000313|EMBL:SDS42900.1,
RC   ECO:0000313|Proteomes:UP000185663};
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; LT629776; SDS42900.1; -; Genomic_DNA.
DR   STRING; 1122933.JNIY01000006_gene1949; -.
DR   Proteomes; UP000185663; Chromosome i.
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   Complete proteome {ECO:0000313|Proteomes:UP000185663};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185663};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      136    211       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      282    319       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       64    151       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1H1S483}.
FT   REGION      212    282       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1H1S483}.
FT   REGION      326    354       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1H1S483}.
FT   COMPBIAS     84    101       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A1H1S483}.
FT   COMPBIAS    102    122       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1H1S483}.
FT   COMPBIAS    221    252       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1H1S483}.
SQ   SEQUENCE   587 AA;  61068 MW;  3B8E432F2A1078D7 CRC64;
     MSDTVQMPAL GESVTEGTVT RWLKSVGDSV EVDEPLLEVS TDKVDTEIPS PVAGTLTKIL
     VEEDETVEVG ADLAVIGDGS GSDSEEEAPA DEPAEEAPQT EEPAPEAEKA PEKDDEPAKE
     DAAPAAESSG GSSGDGEEIT LPALGESVTE GTVTRWLKSV GDTVEVDEPL LEVSTDKVDT
     EVPSPIAGTV QKILVEEDET VEVGAVLAIV GSGAAPAAEP EKAPEPEKEP EPEPEKAPEP
     EKSPEPEPEK APAPKAESSP APEKKPEPTS EKPSGGRSGG SYLTPLVRKL AAQKGVDVES
     VTGTGVGGRI RKEDVLEAAR KAEEAAAAPA AASTGSAPKA PTTVPEVSPL RGTTEKMSRL
     RKIVASRMVE ALQTQAQLTT VVEVDVTRVA KLRAKAKSSF KAREGANLTF LPFFTLAAAE
     ALKAHPNINA SIEDDQIVYH GQENIGIAVD TPRGLLVPVI RDAGDLNLAG IARKIADLGG
     RTRENKVAPD ELGGATFTIT NTGSGGALID TPIVPGGQVA ILGTGTIVKR PVVVTDDEGN
     ESIAVRSMCY IFLSYDHRLV DGADAARFLA TVKNRIEEGA FEAEVGL
//
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