ID Q8YBZ1_BRUME Unreviewed; 308 AA.
AC Q8YBZ1;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:AAL53987.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:AAL53987.1};
GN OrderedLocusNames=BMEII0745 {ECO:0000313|EMBL:AAL53987.1};
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL53987.1, ECO:0000313|Proteomes:UP000000419};
RN [1] {ECO:0000313|EMBL:AAL53987.1, ECO:0000313|Proteomes:UP000000419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094
RC {ECO:0000313|Proteomes:UP000000419};
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA Haselkorn R., Kyrpides N., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; AE008918; AAL53987.1; -; Genomic_DNA.
DR PIR; AH3602; AH3602.
DR AlphaFoldDB; Q8YBZ1; -.
DR KEGG; bme:BMEII0745; -.
DR KEGG; bmel:DK63_2501; -.
DR PATRIC; fig|224914.52.peg.2621; -.
DR eggNOG; COG1249; Bacteria.
DR PhylomeDB; Q8YBZ1; -.
DR Proteomes; UP000000419; Chromosome II.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR22912:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAL53987.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 3..295
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 308 AA; 33039 MW; 7876F4CA82AE2EDA CRC64;
MLVEKTRLGG TCLNVGCIPS KALIHAADEF HRLTTFAAKS PLGITTQNPA IDFARTLEWK
DGIVHRLNSG VAGLLKRSRV RMFQGQARFQ DGKTVLVDTD TGRQTIHAEN IVIATGSVPV
EIQALPFGGN IISSTEALSL EKIPERLAVV GGGYIGLEIG TAFAKLGSRV MVVEATDRIL
PQYDAELTRP VMARLKTLGV EVLTGTSAKG LSADGKALEI RTQDGAVKAI EADKILVTVG
RKPQTDGWGL SEIRLDMDGR FIRIDDRCRT SMRGIYAIGD VTGEPMLAHR AMAQGEMVAE
IIAGGKHA
//
