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Database: UniProt
Entry: A0A2P8W7I2_9CYAN
LinkDB: A0A2P8W7I2_9CYAN
Original site: A0A2P8W7I2_9CYAN 
ID   A0A2P8W7I2_9CYAN        Unreviewed;       359 AA.
AC   A0A2P8W7I2;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:PSN15764.1};
DE   Flags: Fragment;
GN   ORFNames=C7271_20625 {ECO:0000313|EMBL:PSN15764.1};
OS   filamentous cyanobacterium CCP5.
OC   Bacteria; Cyanobacteriota.
OX   NCBI_TaxID=2107701 {ECO:0000313|EMBL:PSN15764.1, ECO:0000313|Proteomes:UP000240885};
RN   [1] {ECO:0000313|EMBL:PSN15764.1, ECO:0000313|Proteomes:UP000240885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP5 {ECO:0000313|EMBL:PSN15764.1,
RC   ECO:0000313|Proteomes:UP000240885};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000240885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP5 {ECO:0000313|Proteomes:UP000240885};
RA   Moore K., Momper L.;
RL   Submitted (MAR-2018) 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:PSN15764.1}.
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DR   EMBL; PYEQ01000507; PSN15764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8W7I2; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000240885; 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; 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; 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   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:UP000240885}.
FT   DOMAIN          13..342
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   NON_TER         359
FT                   /evidence="ECO:0000313|EMBL:PSN15764.1"
SQ   SEQUENCE   359 AA;  39738 MW;  54D35E8C014F44D8 CRC64;
     MRNLKTIEDQ EFDVVIIGGG INGAATARDA ALRGLKTILV EKDDFAGGTT SWSTRLLHGG
     LRYLEYFEFN LVRESLHERE VLLRNAPHLS QPIQMTIPIY RSGSRSYRII QAGMILYDIL
     SYDKSLPNHR MLSRASVRQL FRAIDSDALA GAAQYYDGQA EHAERLCLEN LLDAQQAGAT
     VINYAEVMDI DTGNNRITSL SCRDALSDET FTIKTHAQTV VVNTSGPWVD QVCGLSESAI
     SKGRKIGGTK GSHIIVDPFP GAPEGALYVE AKSDGRPYFI VPWLGQFLIG TTDERYDGKL
     DHIKADDDEI DYLIAETNRV LPAAHLTRND VRFTYSGVRP LPYAEGKKAG SITRAHILH
//
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