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Database: UniProt/TrEMBL
Entry: Q7W630_BORPA
LinkDB: Q7W630_BORPA
Original site: Q7W630_BORPA 
ID   Q7W630_BORPA            Unreviewed;       534 AA.
AC   Q7W630;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:CAE38384.1};
GN   OrderedLocusNames=BPP3097 {ECO:0000313|EMBL:CAE38384.1};
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:CAE38384.1, 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 FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR   EMBL; BX640432; CAE38384.1; -; Genomic_DNA.
DR   RefSeq; WP_010928894.1; NC_002928.3.
DR   AlphaFoldDB; Q7W630; -.
DR   GeneID; 69422478; -.
DR   KEGG; bpa:BPP3097; -.
DR   HOGENOM; CLU_015740_4_1_4; -.
DR   OMA; WAMAPHI; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
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; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          28..388
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          436..515
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          414..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  57138 MW;  691F51B1E3A6B3A9 CRC64;
     MTAPTLAPID PPARAQLLAD LQGAPDWDVI VIGGGATGLG TAVDAAARGY RTLLVEAADF
     AKGTSSKATK LVHGGVRYLA QGNISLVREA LHERGLLNRN APHLVWPLGF VVPAYSLLDQ
     PFYGVGLKMY DMLAGKLNLA PSRWLSRGET LRHAATVAER VNGRALRGGI LYYDGQFDDA
     RLAIALMRTL YDLGGVALNY ARAVGLTRTD GRVDGVTVAD ALGELRVTLR AKCVVNATGV
     WVDAVRRMDD PAAQTMVAPS QGVHLTLPRD FLPGEDAILI PKTDDGRVLF VVPWNGHTIV
     GTTDTPRTDL PLDPQAGQNE IDFILATAAR YLSRKPTRAD VTSVWAGLRP LVKATGEAST
     KSLSREHTIV VSKGGLVTVT GGKWTTYRKM AQDVVDTAIQ HKLLAAAPCR TSELPLHGAP
     TDGQPSGAPH GTPDSYYGTD LATLRALPGA DRMLVKASAL TEAHVRYAAR HELARTVEDV
     LARRNRALFL DAEAALLAAP EVARILAQEL GHDEAWSRAT LAEFEAVAAH YRLA
//
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