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Database: UniProt/TrEMBL
Entry: E3HJ65_ACHXA
LinkDB: E3HJ65_ACHXA
Original site: E3HJ65_ACHXA 
ID   E3HJ65_ACHXA            Unreviewed;       532 AA.
AC   E3HJ65;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase 2 {ECO:0000313|EMBL:ADP16807.1};
DE            EC=1.1.5.3 {ECO:0000313|EMBL:ADP16807.1};
GN   Name=glpD2 {ECO:0000313|EMBL:ADP16807.1};
GN   OrderedLocusNames=AXYL_03487 {ECO:0000313|EMBL:ADP16807.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP16807.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP16807.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP16807.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
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; CP002287; ADP16807.1; -; Genomic_DNA.
DR   RefSeq; WP_013394121.1; NC_014640.1.
DR   AlphaFoldDB; E3HJ65; -.
DR   STRING; 762376.AXYL_03487; -.
DR   KEGG; axy:AXYL_03487; -.
DR   PATRIC; fig|762376.5.peg.3513; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_4_1_4; -.
DR   OMA; GVMTIMN; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000006876; 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:UniProtKB-EC.
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:ADP16807.1}.
FT   DOMAIN          27..387
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          408..513
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   532 AA;  57453 MW;  BD503FDD28594D6A CRC64;
     MNQPLASVAP PDRNRLLNTL DNTHSWDVIV IGGGATGLGT AVDAASRGYR TLLIEGADFA
     KGTSSKATKL VHGGVRYLAQ GNVSLVREAL HERGLLNRNA PHLVWPLGFV VPAYNLFDQP
     FYGVGLKMYD MLAGKLNLAP SRWLSRRDTL ANAPTLAENV QGKNLKGGVL YYDGQFDDAR
     LAMSLMRTLF DLGGTAVNYM RATGLTMTGG KVDGVTVQDA IGGASFTLRA RCVVNATGVW
     VDAVRRMEDK NAQTMVAPSQ GVHLTLPQDF LPGKRAILIP KTDDGRVLFV VPWNGHTIVG
     TTDTPRDDLP LDPQAGAQDV DFILSTAARY LSRKPTRDDV TSVWAGLRPL VKATGEASTK
     SLSREHTILV SKAGLVTVTG GKWTTYRRMA QDVVDTAIQH QLLTQATCRT ESLPLHGAAG
     LAPSQEHAGT PDSYYGSDLP TLKALPGAER MLVKSSGLSE AHVRFAARYE LARSAEDVLA
     RRNRALFLDA EAAMLAAPEV ARILAEELGH DAAWQQRTLQ DLEVVAANYR LK
//
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