(data stored in SCRATCH zone)

SWISSPROT: Q7WAB5_BORPA

ID   Q7WAB5_BORPA            Unreviewed;       591 AA.
AC   Q7WAB5;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 112.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   Name=lpdA {ECO:0000313|EMBL:CAE36766.1};
GN   OrderedLocusNames=BPP1464 {ECO:0000313|EMBL:CAE36766.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-
CC         N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH;
CC         Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-
CC         COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100;
CC         EC=1.8.1.4; Evidence={ECO:0000256|RuleBase:RU003692};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC         ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC       ECO:0000256|RuleBase:RU003692};
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000256|RuleBase:RU003692}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003692}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; BX640427; CAE36766.1; -; Genomic_DNA.
DR   RefSeq; WP_010928051.1; NC_002928.3.
DR   EnsemblBacteria; CAE36766; CAE36766; BPP1464.
DR   KEGG; bpa:BPP1464; -.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; GCEIGQF; -.
DR   BioCyc; BPAR257311:G1GSY-1504-MONOMER; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
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; IPR006258; Lipoamide_DH.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7WAB5.
DR   SWISS-2DPAGE; Q7WAB5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003692};
KW   Lipoyl {ECO:0000256|SAAS:SAAS00065550};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003692,
KW   ECO:0000313|EMBL:CAE36766.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692}.
FT   DOMAIN        4     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   NP_BIND     300    307       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   NP_BIND     438    441       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    564    564       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING     172    172       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     235    235       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000350-
FT                                3}.
FT   BINDING     323    323       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     391    391       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     432    432       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID    163    168       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   591 AA;  61768 MW;  03C4DAD62ACDD7A1 CRC64;
     MSNIVEIKVP DIGDFKEVEV IEVLVAAGDT IKAEQSLITV ESDKASMEIP ASSAGVVKSV
     KVKVGDKVAE GTVILDVEAA GEAAAAPKAE APKAEAPKAD APKAPAAKAS APAAAAYSGS
     ADLECDMLVL GAGPGGYSAA FRAADLGMDT VMVERYATLG GVCLNVGCIP SKALLHNAAV
     IDEARALAAH GISFGEPKVD LDKLRGYKDG VVAKLTGGLA GMARACKVRV ATGTGEFADP
     HHLTVTDGEG KKQTIRFKQA IIAAGSQSVK LPFLPDDERI VDSTGALQLR AIPKKMLIIG
     GGIIGLEMGT VYSTLGARLD VVEMLDGLMQ GADRDLVKVW QKMNAPRFDN IMLKTKTVGA
     EARKDGIYVS FEGEGAPKEP QRYDLVLQAV GRSPNGKKIG AERAGVAVTE RGFIEVDRQM
     RTNVPHIYAI GDVVGQPMLA HKAVHEGHVA AEAAHGEKSF FDARVIPSVA YTDPEVAWVG
     LTEDEAKKQG VKVEKGLFPW AASGRAIANG RDEGFTKLLF DAETHRIVGG GIVGTHAGDL
     ISEIALAIEM GADMVDIGKT IHPHPTLGES VGMAAEVAEG VCTDLPPMRK K
//

If you have problems or comments...

PBIL Back to PBIL home page