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Database: UniProt/TrEMBL
Entry: A9IPD1_BORPD
LinkDB: A9IPD1_BORPD
Original site: A9IPD1_BORPD 
ID   A9IPD1_BORPD            Unreviewed;       532 AA.
AC   A9IPD1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=GlpA protein {ECO:0000313|EMBL:CAP42931.1};
DE            EC=1.1.99.5 {ECO:0000313|EMBL:CAP42931.1};
GN   Name=glpA {ECO:0000313|EMBL:CAP42931.1};
GN   OrderedLocusNames=Bpet2589 {ECO:0000313|EMBL:CAP42931.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42931.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP42931.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP42931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IPD1; -.
DR   STRING; 94624.Bpet2589; -.
DR   KEGG; bpt:Bpet2589; -.
DR   eggNOG; COG0578; Bacteria.
DR   OMA; WAMAPHI; -.
DR   Proteomes; UP000001225; 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,
KW   ECO:0000313|EMBL:CAP42931.1}.
FT   DOMAIN          27..386
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          434..513
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          412..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  56672 MW;  E1CEF1356178DC1E CRC64;
     MNPNPASLPV PGRAALLETL NDNAAWDVIV IGGGATGLGT AVDAASRGYR TLLLEAADFA
     KGTSSKATKL VHGGVRYLAQ GNIALVREAL HERGLLNRNA PHLVWPLGFV VPAYGLFDQP
     FYGIGLKMYD MLAGKLNLSP SRWLSRAETL AQAATVAPSV AGRGLRGGVL YYDGQFDDAR
     LAMALMRTLF DLGGTAVNYV RASGLTRNEK GAIDGVIAQD VLGGGEVTLR ARCVVNAAGV
     WVDSVRRMDD AQAQTMVAPS QGVHLVLPRE FLPGDKAILI PKTDDGRVLF VVPWNGHTLV
     GTTDTPRADL PLDPPATATE VDFILQTAAR YLSRKPTRAD VTSVWAGLRP LVKATGETKT
     LSREHTIVVS RAGLVTVTGG KWTTYRKMAQ DVVDTAIQHQ LLPQAGCRTA DLPLHGAGGA
     PGPDAPAPGT PDSYYGSDLP TLRALPGSEH ILVKASGLTE AHVRFAARHE LARSAEDVLA
     RRNRALFLDS QAALLAAPEV ARILAEELGH DAAWQRATVE DFTRTAAHYR LD
//
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