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Database: UniProt
Entry: A0A1F8KD24_9CHLR
LinkDB: A0A1F8KD24_9CHLR
Original site: A0A1F8KD24_9CHLR 
ID   A0A1F8KD24_9CHLR        Unreviewed;       527 AA.
AC   A0A1F8KD24;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=FAD-dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2X25_00460 {ECO:0000313|EMBL:OGN72171.1};
OS   Chloroflexi bacterium GWB2_49_20.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN72171.1, ECO:0000313|Proteomes:UP000178842};
RN   [1] {ECO:0000313|EMBL:OGN72171.1, ECO:0000313|Proteomes:UP000178842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGN72171.1}.
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DR   EMBL; MGMF01000025; OGN72171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8KD24; -.
DR   STRING; 1797612.A2X25_00460; -.
DR   Proteomes; UP000178842; 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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          20..375
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          415..508
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   527 AA;  58026 MW;  0D2068BBD98B2B46 CRC64;
     MWTTGWRDSL WAGLDQAEWD LIVIGGGITG AGILRESARL GLRCILFEAH DFASGTSSRS
     SKLVHGGLRY LKNAQIRLTS ESVHEREHLL KEGRGLVSPL PFLMANFRED KIPAWAFGIG
     LSVYDLLALK WNHAAYSPAG MRTLCPQLSA PQLVSGFRYF DAVTDDARLV LRVLQEAVTA
     GATALNYARV EGFLKTSRRK VCGVSVCDMA PGAGGRSVEV RGRVVINASG AWADELRCQN
     GGSQRLRILR GSHLFFPWNK LPLTRAVTFL HPQDGRPVFI FPWEGVTLIG TTDVDHHARL
     GTNLSISHAE TGYLMAAIQF AFPDLGLMQS DVQSTLAGVR AVVDTGKANP SKESREFVLW
     MENGLLTVSG GKLTTFRIMA QKALRAVSPL LPERHKLDRG ERVLDPLPAE TSLCDLPAET
     RLRLLGRYAS AACDLASSAR PGEMEPIEAA LPLWAELRWA ARAEGVIHLD DLLLRRVRLG
     IQLPGGGLGQ LNRVRLIVQP ELGWSDERWL QEADAYQNLW QAYYAPV
//
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