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Database: UniProt
Entry: B8KY14_9GAMM
LinkDB: B8KY14_9GAMM
Original site: B8KY14_9GAMM 
ID   B8KY14_9GAMM            Unreviewed;       437 AA.
AC   B8KY14;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=NOR51B_2820 {ECO:0000313|EMBL:EED36867.1};
OS   Luminiphilus syltensis NOR5-1B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Luminiphilus.
OX   NCBI_TaxID=565045 {ECO:0000313|EMBL:EED36867.1, ECO:0000313|Proteomes:UP000004699};
RN   [1] {ECO:0000313|Proteomes:UP000004699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX   PubMed=23705883;
RA   Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT   "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT   OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT   syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT   Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT   halotolerans.";
RL   BMC Microbiol. 13:118-118(2013).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; DS999411; EED36867.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8KY14; -.
DR   STRING; 565045.NOR51B_2820; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_6; -.
DR   Proteomes; UP000004699; 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   ECO:0000313|EMBL:EED36867.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004699};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EED36867.1}.
FT   DOMAIN          11..86
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          154..191
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          89..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  46804 MW;  9289CFD624D9C26F CRC64;
     MNVTEEAGVS TYSFKLPDLG EGIVESEVSA WYVEVGDRVD EDQHIADVQT EKAVVEITAP
     VAGTILALGC PAGEVLAVGV ELVCFDTAGS SNEEPEGANE EPEDEVASSP AQPAPESQQG
     GSKESKPSAV VPRSDPAGFT TETPEGDPAF RQVLASPSLR HRAREAGVNL IDVPGTGPGG
     RIQHKDFEAF LAAGGELVTG QESSRRVAVH EKSISGMRRV IAQKMLDAKR NIPHYSYIEE
     VDVTQIEALR AHLNAHRTED QPKLTLLPFL TAALVRVLPQ FPHCNARFDS EKELLSEYDA
     VHVGFATMTD AGLMVPVVRH CEEQDVWQIA AELSRVSGVA RAGKAKPAEL SGSTITITSL
     GAIGGIATTP IINAPETTII GVNKMQRRAV VIDEQVVIRT MMNLSGSFDH RIVDGYDGAQ
     MIQLLKSFIE NPGAIFV
//
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