ID A0A221R629_9MICC Unreviewed; 588 AA.
AC A0A221R629;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=sucB {ECO:0000313|EMBL:ASN51800.1};
GN ORFNames=CGQ25_06710 {ECO:0000313|EMBL:ASN51800.1};
OS Sinomonas sp. R1AF57.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=2020377 {ECO:0000313|EMBL:ASN51800.1, ECO:0000313|Proteomes:UP000199767};
RN [1] {ECO:0000313|EMBL:ASN51800.1, ECO:0000313|Proteomes:UP000199767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1AF57 {ECO:0000313|EMBL:ASN51800.1,
RC ECO:0000313|Proteomes:UP000199767};
RA Sastre D.E., Santos L., Kagohara E., Andrade L.H.;
RT "Draft Genome Sequence of Sinomonas sp., Isolated from Brazilian Amazon
RT Soils with Potential for Applications in Biocatalysis.";
RL Submitted (JUL-2017) 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}.
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DR EMBL; CP022463; ASN51800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221R629; -.
DR Proteomes; UP000199767; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; 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 NCBIfam; TIGR02927; SucB_Actino; 1.
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; 2.
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; 2.
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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000199767};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ASN51800.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 133..208
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 278..315
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 74..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 60020 MW; 4A45246256D4DD57 CRC64;
MSESVNLPAL GESVTEGTVT RWLKQVGDRV EIDEPLVEVS TDKVDTEIPS PVAGVLEQIL
VAEDETAEVG APLAVIGDGS GSGDSSAAPA AEAAPAAPEP AAQPQDEPAA AAAEQAPAPE
PAEPSVAQAA PDGHEVTLPA LGESVTEGTV TRWLKAVGDA VEVDEPLLEV STDKVDTEVP
SPVAGTLLEI RVGEDETAEV GAVLAVVGSG SAPAPAPAAE PEPAAQPEPA AEPAPAAQAA
PAPAAEPAQA APAAPAAEPA QAAPAAPAAA PAGGESGYVT PLVRKLANQH GIDVTTLTGT
GVGGRIRKQD VLDAAEAKKA ASQQAPAAAP AAAPSAPAQA QPAPAVSSLR GTTEKAPRIR
QVIARRMRES LDISTQLTQV HEVDMTKIAK LRDRAKAQFQ AQNGVKLTFL PFIAKAVAEA
LKQHPKLNAE YDEEAQQITY HNAEHLAIAV DTDKGLLVPV INNAGDLNLA GLAGRIADVA
SRTRSNKIGP DELSGGTFSI TNIGSVGALF DTPIINQPQV AILGTGAIVK RPWVTQNADG
DDVIAIRSMM YLSLTYDHRL VDGADAGRFL QTLRARLEAG AFEADLGL
//
