ID B7QA75_IXOSC Unreviewed; 567 AA.
AC B7QA75;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
DE Flags: Fragment;
GN ORFNames=IscW_ISCW013308 {ECO:0000313|EMBL:EEC15747.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC15747.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC15747.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW013308-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW013308-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|RuleBase:RU361137}.
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|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 -!- SUBCELLULAR LOCATION: Mitochondrion {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; ABJB010079157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010244347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010431857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010729366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010797874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010930833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB011109635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS892726; EEC15747.1; -; Genomic_DNA.
DR RefSeq; XP_002400015.1; XM_002399971.1.
DR AlphaFoldDB; B7QA75; -.
DR STRING; 6945.B7QA75; -.
DR PaxDb; 6945-B7QA75; -.
DR EnsemblMetazoa; ISCW013308-RA; ISCW013308-PA; ISCW013308.
DR KEGG; isc:IscW_ISCW013308; -.
DR VEuPathDB; VectorBase:ISCI013308; -.
DR VEuPathDB; VectorBase:ISCP_022198; -.
DR VEuPathDB; VectorBase:ISCP_023428; -.
DR VEuPathDB; VectorBase:ISCW013308; -.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; B7QA75; -.
DR OMA; TMEFESF; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01349; PDHac_trf_mito; 1.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE 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 1: Evidence at protein level;
KW Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW ECO:0000313|EMBL:EEC15747.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7QA75};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:EEC15747.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 8..84
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 137..213
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 284..322
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 236..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..265
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEC15747.1"
SQ SEQUENCE 567 AA; 60362 MW; 174FC0303FF7320E CRC64;
NSPGLPNYRK VLLPALSPTM ETGTVISWEK KEGDKLNKGD LLCEIETDKS VMSFESPEEG
YLAKIIVPAG TKDIHLGRVL CILVYSEADI AAFGDFESDR TTVPAGQPKA AASAPASAPA
STQMNYIDIP RTSMRQVMLV LLPALSPTME MGTIISWEKK EGDKLNEGDL LCEIETDKAT
MGFETPEEGY LAKIIIPAGT KDVPLGKLLC ILVYDEADVA AFKDFVDDGT AAPTAQPKAA
AAPAAPAPAP APTAAPAPAP ALTPTTPTPS MAGAPAAGVG GRLFASPLAK RLAAEQGLNL
AQIPVGSGPG GRIVAQDLAS AVPMAAAAAP VAAGTKYTDI SLTSMRQTIA KRLLQSKQTI
PHYYLSVDIN MDAVMKLREE FNKAMEKENI KLSVNDFVIK ATALACKKVP QANSSWQETF
IREYKSVDVN MAVSTPEGLI TPIVFGAEKK ARMLLISEET KSLASKARDK KLQPHEFQGG
TITVSNLGMF GVKNFSAIIN PPQACILAVG CTEDVLVPDE NSNTGYRAVK MMSVTLSCDH
RVVDGAVGAQ WLQHFKRLLE RPDLMLL
//
