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
//