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
//