ID E4PM34_MARAH Unreviewed; 532 AA.
AC E4PM34;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ADP97362.1};
DE EC=1.4.3.1 {ECO:0000313|EMBL:ADP97362.1};
GN OrderedLocusNames=HP15_1598 {ECO:0000313|EMBL:ADP97362.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP97362.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP97362.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001978; ADP97362.1; -; Genomic_DNA.
DR RefSeq; WP_014576987.1; NC_017506.1.
DR AlphaFoldDB; E4PM34; -.
DR STRING; 225937.HP15_1598; -.
DR GeneID; 78560202; -.
DR KEGG; mad:HP15_1598; -.
DR PATRIC; fig|225937.3.peg.1609; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_6; -.
DR Proteomes; UP000007077; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0008445; F:D-aspartate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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.
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:ADP97362.1}.
FT DOMAIN 18..371
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 412..505
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 532 AA; 58620 MW; A4E041B3F85CCC79 CRC64;
MTRSEILNAL RSGTNEFDVV VVGGGITGAG VAREAAGSGL RTLLVEQKDF SWGTSSRSSK
MVHGGLRYLG SGHYGLTRDA VRERERLMAE APGLIEPLRF IMPHFKGQFP GPRLFQTLLR
VYDLIARNQS RHFLTPAESM LWVPGLTSEN LAGASGFTDA VTDDSRLVLR LIAEARRDGA
MCLNYTRADE IKRSNGDVSG LLIQAEENDT PIEVFAPLVI NATGAWADRL QSSKTSEDAM
HIRPLRGSHL VLPWSSLPVS CSVSLFHPED GRPVFAFPWL GTTVLGTTDI DHEGSLDQEP
VISESETAYL LEIASRLFPG SPITRNDILS TWAGVRPVVT DGTGKSPSKE NREHALRVDR
GLVSIAGGKL TTFRVIAREA LVQGLGEGSS EVLRPASKPV FQRTDHPSRP ATISYQCWQR
LQGFYGPELD QMLASGPLEP VTPNRATDLL WAELCWACRR EDVQHLDDLL LRRTRLGMVL
PNAGEALLPE IRNHCQPLLG WADQRWEEEQ ARYLSTYHNA YSLPPQEASD AS
//
