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Database: UniProt
Entry: A1ZE93_9BACT
LinkDB: A1ZE93_9BACT
Original site: A1ZE93_9BACT 
ID   A1ZE93_9BACT            Unreviewed;       547 AA.
AC   A1ZE93;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   31-JUL-2019, entry version 66.
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=M23134_04234 {ECO:0000313|EMBL:EAY31401.1};
OS   Microscilla marina ATCC 23134.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Microscillaceae;
OC   Microscilla.
OX   NCBI_TaxID=313606 {ECO:0000313|EMBL:EAY31401.1, ECO:0000313|Proteomes:UP000004095};
RN   [1] {ECO:0000313|EMBL:EAY31401.1, ECO:0000313|Proteomes:UP000004095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23134 {ECO:0000313|EMBL:EAY31401.1,
RC   ECO:0000313|Proteomes:UP000004095};
RA   Haygood M., Podell S., Anderson C., Hopkinson B., Roe K., Barbeau K.,
RA   Gaasterland T., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA =
CC         (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:83100, 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   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAY31401.1}.
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DR   EMBL; AAWS01000003; EAY31401.1; -; Genomic_DNA.
DR   RefSeq; WP_002693977.1; NZ_AAWS01000003.1.
DR   STRING; 313606.M23134_04234; -.
DR   EnsemblBacteria; EAY31401; EAY31401; M23134_04234.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; MMAR313606:G11MJ-806-MONOMER; -.
DR   Proteomes; UP000004095; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 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; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
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:EAY31401.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004095};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:EAY31401.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004095};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:EAY31401.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      122    197       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      264    301       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       85    114       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      214    263       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     90    114       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    218    263       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   547 AA;  58570 MW;  C1C5C841DCE38E1A CRC64;
     MAQIIHMPKM SDTMEEGVIA KWLKKVGDTI QEGDIIAEVE TDKATMELES YDEGTLLYVA
     VEDGGVVPVD GLLAILGAPG EDYKPLLEEN GNGQASSSAT ESAPADETTS APTTTEVTVD
     NATVVTMPKM SDTMEEGVIV SWLKKVGDNI QEGDIIAEVE TDKATMELEA YDEGTLLYVA
     VEEGGSVKVD GLIAVVGEEG ANYQALVDQF KAGGNAQEEA KPTTSASVPK PATSNNGSAP
     KTPTPPNKAA AHASNNANSN GRIKISPLAR KLANEKGYDI GQIQGSGDHG RIIKRDIENF
     TPAAQPAAQD SAVATAPVGT ESYEEINVSQ MRKTIAKRLA SSKFTAPHFY VTMEIRMDAI
     MKARKQINAV SPVKVSFNDI IIKASALAIR KHPKINAYWL EDKIRYNNHI HVGMAVAVKD
     GLFVPVVRFA DNLTFSQVAT TTKDLVSKAK DKKLQPADWE GSTFSVSNLG MFGVEDFTAI
     INPPDSCILA VGGIKQTPVV NDEGQIEVGN IMKVTLSSDH RVVDGALAAS FLKTLKQMIE
     NPYMMLV
//
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