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Database: UniProt
Entry: A0A2G4I519_9BACT
LinkDB: A0A2G4I519_9BACT
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ID   A0A2G4I519_9BACT        Unreviewed;       530 AA.
AC   A0A2G4I519;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:PHX93636.1};
GN   ORFNames=CK546_08350 {ECO:0000313|EMBL:PHX93636.1};
OS   Pedosphaera sp.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX   NCBI_TaxID=2024890 {ECO:0000313|EMBL:PHX93636.1, ECO:0000313|Proteomes:UP000223988};
RN   [1] {ECO:0000313|EMBL:PHX93636.1, ECO:0000313|Proteomes:UP000223988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baikal-G1 {ECO:0000313|EMBL:PHX93636.1};
RX   PubMed=29079621;
RA   Cabello-Yeves P.J., Zemskaya T.I., Rosselli R., Coutinho F.H.,
RA   Zakharenko A.S., Blinov V.V., Rodriguez-Valera F.;
RT   "Genomes of novel microbial lineages assembled from the sub-ice waters of
RT   Lake Baikal.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
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:PHX93636.1}.
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DR   EMBL; NSHY01000171; PHX93636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4I519; -.
DR   Proteomes; UP000223988; 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          37..393
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          442..504
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          424..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  56635 MW;  71F8B092488FF6BD CRC64;
     MKISGGESRS PAVLASLPQV NRAHAISTFL EQPTLWDVLV IGGGATGLGV AVDAAARGLK
     TALVEQGDFA KGTSSRSTKL IHGGFRYLRQ GNIALVRESL RERGLLLRNA PHLVQPLNFV
     VPCYHWWEAP YYGTGLKLYD WFGRELGLAP SRRFSRARTV DAVPNLRTDG LRGGICYQDG
     QFDDARLAIS LAQTAATLGA SVANYVGVVA LLKKEGRICG ARVCDAESGK EFPVHARVVI
     NATGVFTDAV RRMDEASAPP VIAASQGAHL VLPREFLGGD TALMVPRTDD GRVLFAIPWQ
     DRVLVGTTDT AVSETPLEPR PLAGEIHFLL EHAAQYLAKA PAASDILSVT AGLRPLVKLT
     GAKSTAALPR DHVVLVSAGG LVSIAGGKWT TYRKMAADTV DRAMQVAGLP AKPCATERLQ
     LANTRRRSGQ SAAETLPGIG GPRSRRLHPD LSLTADDVLH AARHEMARTV EDVLARRSRA
     LLLNARAAME VAPSVAALLT RGFGHGPVWE AEQITVFREL AKGYLPAQAI
//
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