ID Q7W717_BORPA Unreviewed; 403 AA.
AC Q7W717;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=D-amino acid dehydrogenase small subunit {ECO:0000313|EMBL:CAE38014.1};
DE EC=1.4.99.1 {ECO:0000313|EMBL:CAE38014.1};
GN Name=dadA3 {ECO:0000313|EMBL:CAE38014.1};
GN OrderedLocusNames=BPP2721 {ECO:0000313|EMBL:CAE38014.1};
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:CAE38014.1, 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};
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00009410}.
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DR EMBL; BX640431; CAE38014.1; -; Genomic_DNA.
DR RefSeq; WP_010928696.1; NC_002928.3.
DR AlphaFoldDB; Q7W717; -.
DR GeneID; 69422115; -.
DR KEGG; bpa:BPP2721; -.
DR HOGENOM; CLU_007884_9_2_4; -.
DR Proteomes; UP000001421; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:CAE38014.1}.
FT DOMAIN 3..395
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 403 AA; 44520 MW; 7FC0A7041DBF5E8F CRC64;
MSRIAVIGAG ITGVTTAYAL ALRDHQVTVF DRHRYSAMET SFANGGQLSA SNAEVWNSRS
TLFKGLRWML RRDAPLLLNP RPSWHKYSWL GEFLRQIPRY EANTIETVRL AIAARQHLFD
IAARERIDFD HERRGILHFY ASRREYDSAL RVNALLRAGG LERRPVSPEE MRAIEPALQG
DFYGGFFTES DSTGDIHKFT TGLARAAARH GALFRYETPV SGIDHRGGAI AITTAEAVER
YDKVVICAGV GSRRFASMVG DRVNIYPVKG YSITVSLDDE ASQAGAPWTS LLDDRAKIVT
SRLGAGRFRV AGTAEFNGFN RDIRADRVEP LVAWVRRYFP QVSTSRVVPW AGLRPMLPSM
LPRVGPGKRP GVFYNTGHGH LGWTLSAATA QLVAEAVTAG AGT
//
