ID B8KWX1_9GAMM Unreviewed; 562 AA.
AC B8KWX1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=aceF {ECO:0000313|EMBL:EED34301.1};
GN ORFNames=NOR51B_238 {ECO:0000313|EMBL:EED34301.1};
OS Luminiphilus syltensis NOR5-1B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Luminiphilus.
OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED34301.1, ECO:0000313|Proteomes:UP000004699};
RN [1] {ECO:0000313|Proteomes:UP000004699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX PubMed=23705883;
RA Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT halotolerans.";
RL BMC Microbiol. 13:118-118(2013).
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 -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
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:RU003423}.
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DR EMBL; DS999411; EED34301.1; -; Genomic_DNA.
DR RefSeq; WP_009019049.1; NZ_DS999411.1.
DR AlphaFoldDB; B8KWX1; -.
DR STRING; 565045.NOR51B_238; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000004699; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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; 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 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:RU003423,
KW ECO:0000313|EMBL:EED34301.1}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:EED34301.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004699};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EED34301.1}.
FT DOMAIN 3..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 132..206
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 267..304
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 58576 MW; E57D4A040DE954A4 CRC64;
MSKTNITVPD IGGAEGAEVV EVLVAVGDAI EQEQSLIVLE SDKASMEIPS SHSGTVVELK
VAVGDALSEG DIILVADTGE SASAAEPSEA DTEADTEAAP SDNESAPETA SKDAEEDAAE
EGADDAPAED QERLVPVPDI GTDDDVELIE IVVAEGDAVE EGDSLVVLES DKASMEVPAP
EAGVVTEILV KSGEQVRQGT DIVRLRVKAA SPATPEPKPG SPEEPAKPDD TAVESTPPAA
SQSAAEPAAE PAAGPATADS STGDLAYAGP AVRKLAREFG IDLGNVEGSG PKSRILKEDL
HQFVSGSLKK EPGGPAGAGI PQVPGTDFAK FGEVDAQPRS RLDKLTAANM QRAWLNVPHV
TQFDDADITD LETFRKSLKA EAEQRGTRIT PIPFLLKACA AALNAHPKLK SSLADGGDTL
VHRAYCHIGM AVDTPAGLVV PVVRDVDKKS LWELAEEVIE LATLARDKKL RPDQMQGGVF
SVSSLGNIGG KGFTPIVNTP EVAILGVSRA SEQPVWDGAQ FVPRTLLPLS LSYDHRVVNG
GDAGRFLTDL VGLLGDLRRI LL
//
