ID A0A086A4S0_9FLAO Unreviewed; 530 AA.
AC A0A086A4S0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KFF11684.1};
GN ORFNames=IW15_15870 {ECO:0000313|EMBL:KFF11684.1};
OS Chryseobacterium soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=445961 {ECO:0000313|EMBL:KFF11684.1, ECO:0000313|Proteomes:UP000028705};
RN [1] {ECO:0000313|EMBL:KFF11684.1, ECO:0000313|Proteomes:UP000028705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19298 {ECO:0000313|EMBL:KFF11684.1,
RC ECO:0000313|Proteomes:UP000028705};
RA Stropko S.J., Pipes S.E., Newman J.;
RT "Genome of Chryseobacterium soli DSM 19298.";
RL Submitted (JUL-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFF11684.1}.
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DR EMBL; JPRH01000006; KFF11684.1; -; Genomic_DNA.
DR RefSeq; WP_034713032.1; NZ_JPRH01000006.1.
DR AlphaFoldDB; A0A086A4S0; -.
DR STRING; 445961.IW15_15870; -.
DR eggNOG; COG0578; Bacteria.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000028705; Unassembled WGS sequence.
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; 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..375
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 530 AA; 58628 MW; D315E5FAA806E3DE CRC64;
MKRNEELSKL AGVEEWDFIV IGGGASGLGS ALDATTRGFK TLLLESHDFA KATSSRSTKL
VHGGVRYLAQ GDIGLVKEAL KERGLLAKNA AHVVKNQSFI IPNYTWWGGI YYKIGLSIYD
FLAGKLSLGK TRYISKAQTI SKLPTIEQNN LASGVVYQDG QFDDARLAIN LAQTIIEKGG
SAINYLKVVN LLKNDSNKII GVTAEDQFTQ KQYTIKAKAV VNATGVFTND ILNMNNPKHG
KFVVPSQGIH LVLDKSFLKS NDAIMIPKTS DGRVLFVVPW HDRALVGTTD TLLKDESFEP
RALEEEINFV LETARQYLSK KPTREDVKSV FAGLRPLAAP KGEGKNTKEV SRSHKVITSE
TGLTSIIGGK WTTYRKMAED TIDKAIEIQN LKQTPSVTEH LSIHGNMNAD QVDRSSHLYV
YGSDIPSLQS LQQSNPAYAK KIHPDHEFTI AEAVWAIRHE MAETIEDILA RRVRLLFLDA
RAAIDSAGTI AKLIAEEKNH SPEWIAQQTE EFIALAKGYL LIPYSPRNII
//
