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Database: UniProt/TrEMBL
Entry: A2U1F2_9FLAO
LinkDB: A2U1F2_9FLAO
Original site: A2U1F2_9FLAO 
ID   A2U1F2_9FLAO            Unreviewed;       551 AA.
AC   A2U1F2;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
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=MED152_03345 {ECO:0000313|EMBL:EAQ41717.1};
OS   Polaribacter sp. MED152.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ41717.1, ECO:0000313|Proteomes:UP000006470};
RN   [1] {ECO:0000313|EMBL:EAQ41717.1, ECO:0000313|Proteomes:UP000006470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED152 {ECO:0000313|EMBL:EAQ41717.1};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA   Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
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   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP004349; EAQ41717.1; -; Genomic_DNA.
DR   RefSeq; WP_015480442.1; NC_020830.1.
DR   AlphaFoldDB; A2U1F2; -.
DR   STRING; 313598.MED152_03345; -.
DR   KEGG; pom:MED152_03345; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_10; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000006470; Chromosome.
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:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW   Pyruvate {ECO:0000313|EMBL:EAQ41717.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006470};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          128..203
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          263..300
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          86..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  58541 MW;  C028FCA1066B5021 CRC64;
     MATVINMPRL SDTMEEGVVA QWLVKVGDKV EEGDILAEIE TDKATMEFES FHEGTLLHIG
     IQEGETSPVD KLLAIIGEEG EDISGLLSGE ASSEESDSSA NEANNEEPKE SEAKAEEISE
     GADIPEGVNV ISMPRLSDTM TDGTVATWLK KVGDKVEEGD ILAEIETDKA TMEFECFYEG
     TILHIGVQEG ETAPVDSLLT IIGPEGTDVS AIVKNGGATT SSSSETKSEE TPKKEDSSKT
     ESKTENTQPE ANTTTNSNGG RILASPLAKK IASDKGIDLS KVSGSGENGR IIKKDVENYT
     PAANTNTAAP ATSNATAPVV SIAGEERSEE VKNSQMRKAI AKSLGNSKFS APDFSLNIEV
     DMENAMASRK TINDIPDTKV SFNDMVVKAC AMALKKHPQV NTSWSDNNTI YHSHIHVGVA
     VAVDDGLLVP VIKHTDQLSL TQIGAGVRDL AGKARNKKIA PAEMQGSTFT VSNLGMFGID
     NFTSIINQPN SAILSVGTIV EKPVVKNGQV VVGNTMKLTL TCDHRTVDGA VGAQFLQTLK
     TFIENPVTML A
//
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