ID A2VY12_9BURK Unreviewed; 604 AA.
AC A2VY12;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:EAY64608.1};
GN ORFNames=BCPG_02942 {ECO:0000313|EMBL:EAY64608.1};
OS Burkholderia cenocepacia PC184.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350702 {ECO:0000313|EMBL:EAY64608.1, ECO:0000313|Proteomes:UP000053735};
RN [1] {ECO:0000313|EMBL:EAY64608.1, ECO:0000313|Proteomes:UP000053735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC184 {ECO:0000313|EMBL:EAY64608.1,
RC ECO:0000313|Proteomes:UP000053735};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., Crawford M.,
RA Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., White J.,
RA Larson L., Alvarado L., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA LiPuma J., Lory S.;
RT "The Genome Sequence of Burkholderia cenocepacia (strain PC184).";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CH482378; EAY64608.1; -; Genomic_DNA.
DR AlphaFoldDB; A2VY12; -.
DR HOGENOM; CLU_451779_0_0_4; -.
DR Proteomes; UP000053735; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
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; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
FT DOMAIN 204..504
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 523..603
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 65597 MW; 14DC25CF0C2CF5D1 CRC64;
MGPDAARRPA EPDLCARRAG RSRARGVLHE LPRRAGNVLS RTARLRDVGS LSGPRRIHAL
RAARWPSRPV PARAAYGQAW PEPRRVHRAR HPRSVRRRHA HRPLRLGNAA RPGASSGVVR
VLLVLPESGR RADRVLRGRR RADARMAATR IRTWPDRIRR MGGRRRPRRQ HAAAEEREGA
GRQVHDGAQI VSEANTQEQP APGTVVVIGG GQAAGWVLKT LRAEGFAGRL VMIADEPHLP
YERPPLSKAV LAGDADIETV RVVRPDEFDA LNVEAWQPER AASIDRTRRV VTTESGREIE
YDRLVIATGG TSRRLPDALV KTPHLHYLRT LDEAAALGEK LRASRRVLVI GGGWIGLEVA
ATARKLGVEA VVVEGAPRLC GRSVPQIVSD FLLDLHRSNG VDVRLGAALE SLDAQPDDAS
KVRATLADGT TIDADFAVAG IGLALNASLA SDAGLAVDDG IVVDEYGATS DPAIFACGDV
ANHHNGWLKR RVRLESWANA QNQAIAAAKA VLGVRAPYAE IPWFWSDQYD VNLQILGDLP
ADAQLVVRGD LAARRATLFF VGDGHVRGVI AVNNARELKL ARKWMNQGRA VDTEALADTT
QALA
//
