GenomeNet

Database: UniProt
Entry: Q4A6C7_MYCS5
LinkDB: Q4A6C7_MYCS5
Original site: Q4A6C7_MYCS5 
ID   Q4A6C7_MYCS5            Unreviewed;       622 AA.
AC   Q4A6C7;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 123.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   Name=pdhD {ECO:0000313|EMBL:AAZ43694.1};
GN   OrderedLocusNames=MS53_0275 {ECO:0000313|EMBL:AAZ43694.1};
OS   Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=262723 {ECO:0000313|EMBL:AAZ43694.1, ECO:0000313|Proteomes:UP000000549};
RN   [1] {ECO:0000313|EMBL:AAZ43694.1, ECO:0000313|Proteomes:UP000000549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53 {ECO:0000313|EMBL:AAZ43694.1,
RC   ECO:0000313|Proteomes:UP000000549};
RX   PubMed=16077101; DOI=10.1128/JB.187.16.5568-5577.2005;
RA   Vasconcelos A.T., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O.,
RA   Pinto P.M., Almeida D.F., Almeida L.G., Almeida R., Alves-Filho L.,
RA   Assuncao E.N., Azevedo V.A., Bogo M.R., Brigido M.M., Brocchi M.,
RA   Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S., Carraro D.M.,
RA   de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G.,
RA   Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F., Lopes M.I., Loreto E.L., Madeira H.M.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R., Moreira M.A.,
RA   Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.,
RA   Pedrosa F.O., Pena S.D., Pereira M., Pereira-Ferrari L., Piffer I.,
RA   Pinto L.S., Potrich D.P., Salim A.C., Santos F.R., Schmitt R.,
RA   Schneider M.P., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M., Souza K.R., Souza R.C.,
RA   Staats C.C., Steffens M.B., Teixeira S.M., Urmenyi T.P., Vainstein M.H.,
RA   Zuccherato L.W., Simpson A.J., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) +
CC         N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045,
CC         Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83100; EC=1.8.1.4;
CC         Evidence={ECO:0000256|RuleBase:RU003692};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {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|ARBA:ARBA00007532,
CC       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; AE017245; AAZ43694.1; -; Genomic_DNA.
DR   RefSeq; WP_011283430.1; NC_007294.1.
DR   AlphaFoldDB; Q4A6C7; -.
DR   STRING; 262723.MS53_0275; -.
DR   KEGG; msy:MS53_0275; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_2_14; -.
DR   OMA; DAKYGEW; -.
DR   OrthoDB; 9807946at2; -.
DR   Proteomes; UP000000549; Chromosome.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01350; lipoamide_DH; 1.
DR   PANTHER; PTHR22912:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 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; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692}; Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003692};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000549}.
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          122..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  66204 MW;  FD61C0B6DDC4F28F CRC64;
     MYTFKFADIG EGLHEGVVAE IYVKVGQQVK EGDNLFSVET DKVTSDIPSP VSGTVTAIKM
     AQGDTIHVGQ DIFVFDDGKG DAPVAEAPAP KAEGEEEAAS VVGEVKVNND LIDFSKMFSG
     QPAPKAEEVK PSAAPAPSAE DKTFDEGKKY TGKVDESYDV IVVGSGPGGY LAAEEAGKAG
     LKTLIVEKKY WGGVCLNTGC IPTKTLLKSA DVISYLEHAA DYGIVAEKAK IDFSKSWVKM
     HQRKADVVKK ISSSVEMLMK MSKVTSVFGE AKFVGARALE VNGKVYEAKN VILATGSTAN
     KLLKVPGFES GYKSGEILTS EEAINFDKKL PKKVTIVGGG VIGIEFANVF AKAGSKVTVV
     QNGPVLLPGM DSDVSKLAKE MLEGMGVEVL LNANTLGYEK KTLKVEVDSK TLSLKQDVVL
     TAIGRSANAI NAAEVGVKLG ERGEVLVDSL QRTNVAGVYA IGDVTNQKML AHVAYAHALV
     AVFHILGDKQ KGSYHPKAVP GCVYTSPEIA FIGMTEAEAK AQGRNVMTAK YSFANLGKAI
     ASNKTKGLVK LVVDKEFGEI LGAWMVGENV TDYIAEVAMA MENEISVHEI AHTIHPHPTY
     NEMIWEAARS ASLTLTLAAM KK
//
DBGET integrated database retrieval system