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}.
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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
//