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Database: UniProt
Entry: D5BXT8_NITHN
LinkDB: D5BXT8_NITHN
Original site: D5BXT8_NITHN 
ID   D5BXT8_NITHN            Unreviewed;       897 AA.
AC   D5BXT8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Nhal_2782 {ECO:0000313|EMBL:ADE15849.1};
OS   Nitrosococcus halophilus (strain Nc4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE15849.1, ECO:0000313|Proteomes:UP000001844};
RN   [1] {ECO:0000313|Proteomes:UP000001844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG   US DOE Joint Genome Institute;
RA   Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA   Klotz M.G.;
RT   "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT   aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR   EMBL; CP001798; ADE15849.1; -; Genomic_DNA.
DR   RefSeq; WP_013033706.1; NC_013960.1.
DR   AlphaFoldDB; D5BXT8; -.
DR   STRING; 472759.Nhal_2782; -.
DR   KEGG; nhl:Nhal_2782; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_300138_0_0_6; -.
DR   OMA; EYSNPTF; -.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000001844; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001844};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          4..79
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          135..172
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          86..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   897 AA;  95588 MW;  185A86CA153E2538 CRC64;
     MAEPYVIKMP QLSDTMTEGV LVSWEKEIGE FIERGTVVAT VETDKAIMDV EVFREGYLSG
     PQLPVDGVAA VGEPIAYLVA EAEQVEKTEA SASPQPAPEA EERPKFEPAG TSKPKTKIPA
     MPGGATPAPH PSHTRATPYA RQLAGAHAID LAGMKGSGPD GVIVAADVVS GQGARGMTRR
     IFEVPGTGRP MDSMEKAIAH NMEYSLSMPL FRATVYVDPS RLVAAAKEQG SSVTVALAKA
     AALAVEEHPK INSVYQHEDR ILEREQVDVG LAVATEGMGL VVPVLRDTSN RNLAELSASW
     ADLVERARIK RLKPEEYSNP TFVISNMGML GVAYFDAIPS PGTSAILAIA TTGSQGMPVT
     ITADHRIVNG ADAARFLNTF KERVESPETW ISGGSASPST AKEALPLEGD WDYDVVVIGG
     GPGGEDCARE LAEHGIKVAL INDSPFPGGE CLWRGCIPSK TWRAAADRIR DRAHDSHLGV
     GGTTPAALNW KALEATRRHV LQSRGEMALK TDKGMKIKFI QGHARFADEH HLVVDTSGNS
     EDPFARTQPT QPDSQGQRIS FAGAVIATGA PPFIPPIPGA QEGVQAGGVL TSDTVWGLER
     VPERLAVIGG GAIGVEMAQI FQDFGTEVLL LEAQERLLAE VEPEVGKLLA EILNADPRLT
     VQSSAKVQAI SGQPGAMQVA FDDSEGTSHR LEVDYVLMAT GKRPNLEPLA LDQAGVAIAN
     GVIQVDAQCT TSKSHIFAVG DVIGGLMLAH TAGQQGRVAA ATILGEPHAY ELEKDCGVIF
     TRPQAAFVGL SVAQAKERGV DAAEVKMPIR IDAKAMINNE TEGLIKIVAD KASHRIIGVH
     FLADHADTLI GEAVMMVTGK MTLEQVARAI HPHPTQTELF GEMARRLLSR LRRTQRR
//
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