ID N8WYI8_9GAMM Unreviewed; 675 AA.
AC N8WYI8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=F969_00865 {ECO:0000313|EMBL:ENU99964.1};
OS Acinetobacter variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70346 {ECO:0000313|EMBL:ENU99964.1, ECO:0000313|Proteomes:UP000013070};
RN [1] {ECO:0000313|EMBL:ENU99964.1, ECO:0000313|Proteomes:UP000013070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 899 {ECO:0000313|EMBL:ENU99964.1,
RC ECO:0000313|Proteomes:UP000013070};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 899.";
RL Submitted (FEB-2013) 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 -!- 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}.
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:ENU99964.1}.
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DR EMBL; APPE01000041; ENU99964.1; -; Genomic_DNA.
DR RefSeq; WP_004781497.1; NZ_KB849402.1.
DR AlphaFoldDB; N8WYI8; -.
DR PATRIC; fig|1217710.3.peg.818; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR Proteomes; UP000013070; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 3.
DR Gene3D; 2.40.50.100; -; 3.
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; 3.
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; 3.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
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 Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ENU99964.1}.
FT DOMAIN 1..73
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 131..204
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 246..319
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 377..414
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 71045 MW; E5E1A4436DADCB6E CRC64;
MQITTPDIGV DKATVAEILV KVGDTIAVDE SIVLLESDKA SVEVPSTSAG VVKSILINQG
DEVSEGIVLI ELQAEDDAGT VESQEADAAD KTSENTPTEL PDEEILQEVA THQPKASSQN
EQSSQSTSTS TVEVKLPDIG VEKALVGEIL VQVGDEVEVD QSLVVVESDK ATVEVPSTVA
GTVEAIHIQE GDSVKEGVLI LTVKTTDSAP AAEQAAPQAE EKPKAQATPE VKTETAPQQA
ASPAGDIEVK VPDLGVDKAA VAEILVQVGD TVEKDQSIIV VESDKATVEV PSTTAGVIKA
IHVELGQNVS EGVALITIEA EGQAAPAAPA EKSEAPAAKA TPAPAAAPKA DTAAVTPEMH
SADKLSKEQN AANAKVYAGP AVRKLARELG VVLAEVKASG PHERLMKEDL FAYVKDRLTA
PQTTAAPAAA AAPAGLPKLP DFSAFGGVEE KALTRLQQVS IPQLSLNNYI PQVTQFDAAD
ITELEAWRNE LKGNFKKEGI GLTIMAFIIK AVAYLLKEER EFAGHLSDDG KSVLLRNEIH
MGIAVATPDG LTVPVLRNPD QKSIKQIAIE LGELSQKARD KKLSPKDLQG ANFTITSLGS
IGGTAFTPLV NWPQVAILGI SPATMQPVWN GESFDPRLML PLSLSYDHRV INGADAARFT
NKLTKLLKDI RTLLI
//
