ID M2U819_9SPHN Unreviewed; 474 AA.
AC M2U819;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=C725_0062 {ECO:0000313|EMBL:EMD84132.1};
OS Pacificimonas flava.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingosinicellaceae; Pacificimonas.
OX NCBI_TaxID=1234595 {ECO:0000313|EMBL:EMD84132.1, ECO:0000313|Proteomes:UP000011717};
RN [1] {ECO:0000313|EMBL:EMD84132.1, ECO:0000313|Proteomes:UP000011717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2015 {ECO:0000313|EMBL:EMD84132.1,
RC ECO:0000313|Proteomes:UP000011717};
RX PubMed=23661488;
RA Tang K., Liu K., Li S., Jiao N.;
RT "Draft Genome Sequence of Strain JLT2015T, Belonging to the Family
RT Sphingomonadaceae of the Alphaproteobacteria.";
RL Genome Announc. 1:E00226-13(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}.
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:EMD84132.1}.
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DR EMBL; AMRV01000001; EMD84132.1; -; Genomic_DNA.
DR RefSeq; WP_008599431.1; NZ_JACHGC010000002.1.
DR AlphaFoldDB; M2U819; -.
DR PATRIC; fig|1234595.3.peg.62; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000011717; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:EMD84132.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000011717};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EMD84132.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 187..224
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 83..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 49767 MW; 918FBA8CFA4A9405 CRC64;
MGEHVIKLPD VGEGVAEAEL VEWEVKVGDQ VLEDQVLAAV MTDKATVEIP APRDGKVIWL
GAEIGDIIAV GSPIVRMEVE GQGNVKPGEE LPAEENEPAA EARDGPESPS EPQSPGEAAR
AKEGAPSDKA DFAEPEAARP SPKPAGTGGG ASTSTAPQES GTKPAGSGSA AAAADTGLPR
AIGEKPLASP AVRRRAQDGG IDLRRVAGSG PAGRITNDDL DTFIAAGGAP AATGGSVRAR
DMSVEEIKVV GLRRKIAEKM STSKSRIPHI TYVDEVDVTA LEDLRAKLNR EKSGSKPKLT
LLPFLMRAMA RAIAEQPQMN SLYDDEAGIV RRYGGMNMGV AAQTDKGLVV PVVRHVEALS
IWDCAGELNR LADAAKNGTA SREELTGATI TITSLGAMGG IVTTPVINHP EVAIVGVNKM
RVMPVWQDGQ FVPRKMMNLS SSFDHRVIDG WDAAVFIQRI KGLLEAPASI FIED
//