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Database: UniProt
Entry: X2H6Y5_9NEIS
LinkDB: X2H6Y5_9NEIS
Original site: X2H6Y5_9NEIS 
ID   X2H6Y5_9NEIS            Unreviewed;       546 AA.
AC   X2H6Y5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   ORFNames=SALWKB2_0788 {ECO:0000313|EMBL:AHN28170.1};
OS   Snodgrassella alvi wkB2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Snodgrassella.
OX   NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN28170.1, ECO:0000313|Proteomes:UP000019668};
RN   [1] {ECO:0000313|EMBL:AHN28170.1, ECO:0000313|Proteomes:UP000019668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WkB2 {ECO:0000313|EMBL:AHN28170.1};
RX   PubMed=25053814;
RA   Kwong W.K., Engel P., Koch H., Moran N.A.;
RT   "Genomics and host specialization of honey bee and bumble bee gut
RT   symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000925,
CC         ECO:0000256|RuleBase:RU361137};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|ARBA:ARBA00011484,
CC       ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP007446; AHN28170.1; -; Genomic_DNA.
DR   RefSeq; WP_025330389.1; NZ_CP091515.1.
DR   AlphaFoldDB; X2H6Y5; -.
DR   STRING; 1196094.SALWKB2_0788; -.
DR   GeneID; 32536181; -.
DR   KEGG; salv:SALWKB2_0788; -.
DR   PATRIC; fig|1196094.4.peg.788; -.
DR   HOGENOM; CLU_016733_10_0_4; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000019668; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; 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; IPR006256; AcTrfase_Pyrv_DH_cplx.
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; TIGR01348; PDHac_trf_long; 1.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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:RU361137,
KW   ECO:0000313|EMBL:AHN28170.1};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW   Pyruvate {ECO:0000313|EMBL:AHN28170.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:AHN28170.1}.
FT   DOMAIN          4..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          111..185
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          247..284
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   546 AA;  57962 MW;  D5FC4D41A565EB7B CRC64;
     MSQIVEIKVP DIGNYTGVDV IDVAVKVGDS IAVDDTLITL ETDKATMDVP ADKAGVVKEV
     LVKVGDKVSE GNVIVKVETS AAASASSSAG TTTEAPVKAT TTEAAGTAAQ SVAVKVPDIG
     NFSNVDVIEV DIKVGDDVAV DQTLVTLETD KATMDVPSTV AGKVTAVHVK VGDKVSEGSA
     LIEVAVAPAS AAAAPLTPEQ KEASEIKKQV AATPSAENNE LRAEIKSHVP QAFGSSDIDE
     KGFEKAHASP SVRKLARELG VDLGRVSGSG RKGRITPVDL REFVKSVMQK VDRGGSGASL
     GGGLDLLPWP KVDFSKFGEI EVKELSRIKK ISGQNLARNW VMIPHVTLHE DADMTDLEAF
     RKQLNKEWER AGIKVSPLAF IILACVKALQ EFPEFNSSLD GDNLILKKYI HIGFAADTPN
     GLVVPVIKNA DQKGLKEITQ ELADMSKRAR EGKLKPQEMQ GASFTISSLG GIGGTGFTPI
     VNAPEVAILG VCKSQIKPTW NGKEFEPRLQ CPLSLSFDHR VIDGAAGMRF LVFISQLLAD
     FRRVSL
//
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