ID A5FA78_FLAJ1 Unreviewed; 525 AA.
AC A5FA78;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ABQ07884.1};
GN OrderedLocusNames=Fjoh_4885 {ECO:0000313|EMBL:ABQ07884.1};
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ07884.1, ECO:0000313|Proteomes:UP000006694};
RN [1] {ECO:0000313|EMBL:ABQ07884.1, ECO:0000313|Proteomes:UP000006694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC UW101 {ECO:0000313|Proteomes:UP000006694};
RX PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ07884.1; -; Genomic_DNA.
DR RefSeq; WP_012026850.1; NZ_MUGZ01000004.1.
DR AlphaFoldDB; A5FA78; -.
DR STRING; 376686.Fjoh_4885; -.
DR KEGG; fjo:Fjoh_4885; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_4_1_10; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000006694; 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: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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 17..374
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 364..502
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 525 AA; 58469 MW; 1629A13E5754C0DF CRC64;
MNRSEQLLKL QNTENWDVII IGGGASGLGT AIDAASRGYK TILLEAVDFA KGTSSRSTKL
VHGGVRYLAQ GDVHLVREAL KERGLLAQNA NHLVKNQSFV IPNYHWLSGY FYTIGLKIYD
LLSGGLSLGS SKYLSKKKTI EMLPNVEEDG LVNGVIYHDG QFDDSRLAVN LAQTAVENGA
CVLNYTKVIN LIKDDKNQIT GVQAVDQETG INYNIKGAVV INATGVFTNA IMKLNDKVYK
KYIVPSQGIH LVFDKSFLPG EHALMIPKTK DGRVLFAVPW HNHVVVGTTD TLIKKQSLEP
IALESEIEFV LETAQRFLAK KPTRADVLSV FAGLRPLAAP KEEGRSTKEV SRSHKIIVSE
TGLITITGGK WTTYRKIAED IIDKAILKGK LPKKPCITQN LSIHGNKPTT TLDRENHLYI
YGSDITKILQ LQEKEPELKE KLHLDYEFTL AEIVWAVRYE MARTVDDILA RRVRLLFLDA
RAAIEVSEKT ARVIAKELGH DENWVAKEIA DFKATSKGFF LSEFR
//
