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Database: UniProt
Entry: A0A179DMJ2_9SPHI
LinkDB: A0A179DMJ2_9SPHI
Original site: A0A179DMJ2_9SPHI 
ID   A0A179DMJ2_9SPHI        Unreviewed;       462 AA.
AC   A0A179DMJ2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=A5893_03905 {ECO:0000313|EMBL:OAQ42265.1};
OS   Pedobacter psychrophilus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1826909 {ECO:0000313|EMBL:OAQ42265.1, ECO:0000313|Proteomes:UP000078459};
RN   [1] {ECO:0000313|EMBL:OAQ42265.1, ECO:0000313|Proteomes:UP000078459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ42265.1,
RC   ECO:0000313|Proteomes:UP000078459};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAQ42265.1, ECO:0000313|Proteomes:UP000078459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ42265.1,
RC   ECO:0000313|Proteomes:UP000078459};
RA   Svec P.;
RT   "Pedobacter psychrophilus sp. nov., isolated from Antarctic fragmentary
RT   rock.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAQ42265.1}.
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DR   EMBL; LWHJ01000011; OAQ42265.1; -; Genomic_DNA.
DR   RefSeq; WP_068821294.1; NZ_LWHJ01000011.1.
DR   AlphaFoldDB; A0A179DMJ2; -.
DR   STRING; 1826909.A5893_03905; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000078459; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 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   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078459};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          141..181
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          181..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  50908 MW;  192969BE5C89B232 CRC64;
     MAQYELLLPK MGESVAEATV IRWEKNPGDN IAIDDTILEI ATDKVDSEVP SPVSGKMVKH
     LFNENDVAQV GDVIAIIEIE SDTAVAEEVK DAELESLEKA TEIPFVPEEK EETIEDKVEE
     VKTEETDEVK QPNNFSSSDR FYSPLVKSIA QEEGISVEQL DNIKGSGSEG RVTKDDLLDF
     ISSKNNNNSQ TKDQINTTSS QEPVESKKQE TPATEPAKVV QPVAKSGGDE IIEMDRMRKL
     IADHMVSSKQ TSPHVTSFIE VDVTNMVNWR NKVKTSFEKR EGEKITFTPI FVEAVAKALK
     DLPMVNVSVK GSQIIKKKDI NIGMATALPS GNLIVPVIKN ADQLNLVGLT KSVNDLARRS
     RANKLLPDEV QGGTFTVTNL GTFDNTMGTP IINQPQVAIL AVGAIKKKPA VLETEYGDVI
     AIRHLMYLSM SYDHRVVDGS LGGMFIKKVA DNLEQWDVNR EI
//
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