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Database: UniProt
Entry: F0KHB8_ACICP
LinkDB: F0KHB8_ACICP
Original site: F0KHB8_ACICP 
ID   F0KHB8_ACICP            Unreviewed;       662 AA.
AC   F0KHB8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
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:ADY83379.1};
GN   OrderedLocusNames=BDGL_002793 {ECO:0000313|EMBL:ADY83379.1};
OS   Acinetobacter calcoaceticus (strain PHEA-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY83379.1, ECO:0000313|Proteomes:UP000007477};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PHEA-2;
RA   Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT   "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT   Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT   environmental adaptation.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY83379.1, ECO:0000313|Proteomes:UP000007477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY83379.1,
RC   ECO:0000313|Proteomes:UP000007477};
RX   PubMed=21441526; DOI=10.1128/JB.00261-11;
RA   Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA   Yuan M., Zhou Z., Elmerich C., Lin M.;
RT   "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT   industry wastewater.";
RL   J. Bacteriol. 193:2672-2673(2011).
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; CP002177; ADY83379.1; -; Genomic_DNA.
DR   RefSeq; WP_014207930.1; NC_016603.1.
DR   RefSeq; YP_004997061.1; NC_016603.1.
DR   AlphaFoldDB; F0KHB8; -.
DR   STRING; 871585.BDGL_002793; -.
DR   GeneID; 11637440; -.
DR   KEGG; acc:BDGL_002793; -.
DR   PATRIC; fig|871585.3.peg.2792; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_6; -.
DR   OMA; HPCIMAP; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000007477; Chromosome.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd06849; lipoyl_domain; 3.
DR   Gene3D; 2.40.50.100; -; 3.
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; 3.
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; 3.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR   PROSITE; PS00189; LIPOYL; 3.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:ADY83379.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007477};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          1..73
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          119..192
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          232..305
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          364..401
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          80..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   662 AA;  68643 MW;  5BA051C5818AFC25 CRC64;
     MQIKTPDIGV DKAVVAEILV KVGDSIAEND SLVLLESDKA SVEVPSTSAG VVKSILIKEG
     DSVAEGTVLL ELEAEGAAPV AQAEEAPKAA PAAEQTAAPA AAQQPSTAAQ PATATTSQVV
     EVQVPDIGVE KALVGEILVK VGEQIDVEQS IVVVESDKAT VEVPSSVAGT VESIQVKEGD
     TVKEGVVLIK VKTTSASSAP AEAPASTTAA PAAAPAPAQQ ETVASTATQS GPVDINVPDL
     GVDKAVVAEI LVQVGDKVDV DQSLVVVESD KATVEVPSTV AGVVKAIHLQ AGQQVSQGVL
     LATIEAEGQA PAAAPAAKAE SAPAQQAAAP KAAAPAPTQA VSAPASSGND KLTKEQEAEN
     AKVYAGPAVR KLARELGVVL SQVKTSGEHG RVVKEDIFAY VKTRLTAPQA APVASAAPAV
     SGLPKLPDFT AFGGVEEKVL TRLQQVSIPQ LSLNNFIPQV TQFDLADITE LEDWRNELKG
     NFKKEGVSLT IMAFIIKAVA YLLKEEREFA GHLSDDGKSV LLRNEIHMGI AVATPDGLTV
     PVLRNPDQKS IKQIAVELGM LGQKARDKKL TPKDLQGANF TISSLGAIGG TAFTPLVNWP
     QVAILGISPA TMQPVWNGKD FDPRLMLPLS LSYDHRVING ADAARFTNKL TKLLKDIRTL
     LI
//
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