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
//