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Database: UniProt
Entry: A0A1M3K918_9CHLR
LinkDB: A0A1M3K918_9CHLR
Original site: A0A1M3K918_9CHLR 
ID   A0A1M3K918_9CHLR        Unreviewed;       554 AA.
AC   A0A1M3K918;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=FAD-dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGO78_02445 {ECO:0000313|EMBL:OJX43843.1};
OS   Chloroflexi bacterium 44-23.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1895927 {ECO:0000313|EMBL:OJX43843.1, ECO:0000313|Proteomes:UP000184201};
RN   [1] {ECO:0000313|EMBL:OJX43843.1, ECO:0000313|Proteomes:UP000184201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-23 {ECO:0000313|EMBL:OJX43843.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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}.
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:OJX43843.1}.
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DR   EMBL; MKUW01000013; OJX43843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3K918; -.
DR   STRING; 1895927.BGO78_02445; -.
DR   Proteomes; UP000184201; 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: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}.
FT   DOMAIN          17..357
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          415..540
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   554 AA;  61950 MW;  9D4B887F60B12FD3 CRC64;
     MDRKTIIESL KMNPEIDALV VGAGINGAGV FRDLALNGVN VLMIDRGDFC SGTSAASSHM
     AHGGIRYLEN GEFGLVREAV AERNRMIENA PHLVQPLPTV IPIFKIWSGL LNAPLKFVNL
     LDRPSERGAL VIKIGLIFYD SFTRKQKTVP THKFFGRSEA LARYPYLNEK IKYAALYFDG
     ELLSPERMTV EIILDGEDEG DHAKALNYAS FHKVENGQVI IKDEETGQLI TVKPKVIINA
     AGPWIDYVNQ DAGIITKYIG GTKGSHLVIK NEELRKAVGV SEFFFENKDG RIVLCLPFHD
     KVIVGTSDLP IDNPDDAYCT PEEEEYFIEL VSRVFPTIKI TRDQIVFRFS GVRPLEYQEA
     KTTGQITRDH SIKEDTIEGM PLLSLVGGKW TSFRAFSEQV ATKTLETLGK TRAKSTESLP
     IRGGENLPLT KEAKEAYVTN LVATFGLAED YAKELLRRYG TYAVKIAAFI QENQGKTLTS
     IPNWNSGELV YILQNEKPLH LDDLFIRRST IAWLGNATPP VIEEFAEIMA NEYGWSAEKK
     KEEIDRVLSV IEKS
//
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