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Database: UniProt
Entry: B0RC06_CLAMS
LinkDB: B0RC06_CLAMS
Original site: B0RC06_CLAMS 
ID   B0RC06_CLAMS            Unreviewed;       482 AA.
AC   B0RC06;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 101.
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:CAQ01734.1};
GN   OrderedLocusNames=CMS1624 {ECO:0000313|EMBL:CAQ01734.1};
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ01734.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ01734.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ01734.1; -; Genomic_DNA.
DR   RefSeq; WP_012298990.1; NZ_MZMN01000003.1.
DR   AlphaFoldDB; B0RC06; -.
DR   STRING; 31964.CMS1624; -.
DR   KEGG; cms:CMS1624; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_1_11; -.
DR   OMA; MKVPSPG; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000001318; Chromosome.
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; 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; 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:CAQ01734.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CAQ01734.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          182..219
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          78..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..124
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..168
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  49390 MW;  29030319A54FABC0 CRC64;
     MSESVNLPAL GESVTEGTVT RWLKNVGDHV EVDEPLLEVS TDKVDTEIPS PVAGVIEEIL
     VQEDETVEVG AVLVRIGDGS GGGDAPAEEP AAEQAAEPEP AADEAVEDTV IPSTEAEDDA
     EAPAPVEPEP APAAEQPDPE PTPAPAPAAP APVAATPAPA PAAAAPAPAA APAPAASGNA
     GYVTPLVRKL ANERGVDVSS VVGTGVGGRI RKEDVLAAAE AAASKSAPTA SAPAAPAAAP
     LETSPLRGTT AKMSRMRKLI ADRAVVSMQS TAQLTSVVEV DVTKVARFRD RVKGDFLEKT
     GVKLSFLPFF ALAAAEALKA YPVVNATVDG DSIVYPDHEN ISIAVDTERG LLTPVVKNAE
     GKNLAQFASE IADLAARTRD NKLSPDELAG GTFTLTNTGS RGALFDTPVV FLPQSAILGT
     GIVTKRPVVI TADGQDTIAI RSTVYLALSY DHRIVDGADA SRFLVAVKNR LEAGAFDADL
     GI
//
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