ID A0A127VFN6_9SPHI Unreviewed; 535 AA.
AC A0A127VFN6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:AMQ00100.1};
GN ORFNames=AY601_3229 {ECO:0000313|EMBL:AMQ00100.1};
OS Pedobacter cryoconitis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMQ00100.1, ECO:0000313|Proteomes:UP000071561};
RN [1] {ECO:0000313|EMBL:AMQ00100.1, ECO:0000313|Proteomes:UP000071561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMQ00100.1,
RC ECO:0000313|Proteomes:UP000071561};
RA Lee J., Kim O.-S.;
RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL Submitted (MAR-2016) 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; CP014504; AMQ00100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127VFN6; -.
DR KEGG; pcm:AY601_3229; -.
DR PATRIC; fig|188932.3.peg.3364; -.
DR Proteomes; UP000071561; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000071561}.
FT DOMAIN 27..385
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 420..511
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 535 AA; 59138 MW; 15E59943C4141B95 CRC64;
MIRRPLHMNT SRKELIGNIV DPEKVWDVIV VGGGATGLGA ALDAASRGYQ TLLLEQADFA
KGTSSRSTKL VHGGVRYLAQ GDIGLVREAL YERGLLLKNA AHLVKNESFI IPNYEWWGGA
FYTIGLTLYD LLAGKLGFGR ARHISKKEVI SKLATIQPDH LYGGVVYHDG QFDDSRLAVN
LAQTSLEQGA TILNYIRVTS LIKDAQDKVA GVVATDIESD ITYQLKGKTV INATGVFVDD
LLQMDKPGKK PLVRSSQGVH LVIERSFMPG EDAIMIPKTD DGRVLFVVPW HDKLVVGTTD
TPLDQHSLEP VALEEEIEFI MRTAAKYLVK APTRKDVLSV FAGLRPLAAP EDGSSKTKEI
SRSHKLIVTT SGLITITGGK WTTYRRMGED TINKAIEVGK LPARPTKTKE LSIHGSKANV
NRNDHLYVYG SDEAGVLALG DENPAWKEKL HARLPYLQAE VIWGVRYEMA RTVEDILARR
VRALFLDARA AIDMAPAVAK LVATELQYDE AWENEQVKTF RKLAQSYLLE PYTPE
//
