ID Q7W6R7_BORPA Unreviewed; 409 AA.
AC Q7W6R7;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:CAE38126.1};
GN OrderedLocusNames=BPP2834 {ECO:0000313|EMBL:CAE38126.1};
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311 {ECO:0000313|EMBL:CAE38126.1, 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.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., 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., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; BX640431; CAE38126.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7W6R7; -.
DR KEGG; bpa:BPP2834; -.
DR HOGENOM; CLU_003291_4_0_4; -.
DR Proteomes; UP000001421; Chromosome.
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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
FT DOMAIN 5..299
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 318..392
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 409 AA; 43755 MW; 6866118325F983C5 CRC64;
MAMDSIAIIG AGQAGAALAA RLRQAGFQGG IDVFGAESAP PYQRPPLSKK YLAGDWEQER
LWLRPAQFWR EQGIALHLGG TVEALDLASR TLRCGGRRHG WRKLALTTGA APRPLPAAFA
GRSNVFELRN LADVQRLQPA FLAGRRLLVL GGGYIGLETA AVAAQAGLSV QVVERASRVL
ERVACPATAA AIRALHQRHG VLIHEGRTVA GTEGDEALTG VELDNGLRIA CDLVVAGVGV
APQTALAEAA GIDCDDGILV DAYGRTSAPD VWAAGDCARF VLGGEPARLE SVQNAIDQAE
AVADDMLGQG RPYQPVPWFW SDQYDMKLQI VGLNRGYDAV VSHASAKGES HWYFRADRLI
SVDALNDGRA YMVGKKLLEA GRAVGRGEVE RPGFEPMQLL RDQAESRLR
//
