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Database: UniProt
Entry: A0A2C7ACC2_9PROT
LinkDB: A0A2C7ACC2_9PROT
Original site: A0A2C7ACC2_9PROT 
ID   A0A2C7ACC2_9PROT        Unreviewed;       502 AA.
AC   A0A2C7ACC2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=CR162_09080 {ECO:0000313|EMBL:PHK95313.1};
OS   Pseudoroseomonas rhizosphaerae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Pseudoroseomonas.
OX   NCBI_TaxID=1335062 {ECO:0000313|EMBL:PHK95313.1, ECO:0000313|Proteomes:UP000223527};
RN   [1] {ECO:0000313|EMBL:PHK95313.1, ECO:0000313|Proteomes:UP000223527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YW11 {ECO:0000313|EMBL:PHK95313.1,
RC   ECO:0000313|Proteomes:UP000223527};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC       ECO:0000256|RuleBase:RU361217}.
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:PHK95313.1}.
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DR   EMBL; PDNU01000012; PHK95313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C7ACC2; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000223527; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 6.10.250.1890; -; 1.
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; PS00977; FAD_G3PDH_1; 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   ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223527}.
FT   DOMAIN          7..330
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          386..486
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   502 AA;  54776 MW;  2A400AAF2C97A43D CRC64;
     MAHDNVDLLV IGGGANGAGI ARDAAGRGLS VLLAERGDLG GATSSASSKL VHGGLRYLEH
     YEFRLVREAL GEREVLLRLA PHIVWPMRFV LPHVEGMRPR WMLRAGLFLY DNLARRVTLP
     ASQALDFRAH PWGGPLNGQS RHGFAYSDAW VEDARLVILN ARDAAARGAT ILVRTAFTGA
     TRDAEGWTAT LREENGQERV VRARAIANAA GPWVMEALGE TGVTTKDRIR LVRGSHIVVP
     ALYEGDQAYI LQNDDRRVVF VIPYEGRFTL IGTTDVPHDP ASGPPRCTPE EAAYLCRAVS
     RQFRRPVTPE DIVWSYSGVR PLHDDGAENP SAVTRDYVLK MDRPAGRGGA PLLSVFGGKI
     TTYRRLAEDA AGQIAAALGH GGGAWTAGAT LPGGDLGGLS SEAFLAEAER RYPFLPPPQL
     RRLFHCYGGE LDAVLGHAGS LADLGRDLGG GITERELAWM MREEWVRAPE DALWRRTKRG
     LHMTEAERRN FAQAFPEVRQ AA
//
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