UniProt/TrEMBL: R1GER7

Database: UniProt/TrEMBL
Entry: R1GER7_BOTPV

LinkDB:  R1GER7_BOTPV 
Original site:  R1GER7_BOTPV

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   R1GER7_BOTPV            Unreviewed;       730 AA.
AC   R1GER7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN   ORFNames=UCRNP2_3123 {ECO:0000313|EMBL:EOD50095.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD50095.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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}.
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DR   EMBL; KB916013; EOD50095.1; -; Genomic_DNA.
DR   RefSeq; XP_007582421.1; XM_007582359.1.
DR   AlphaFoldDB; R1GER7; -.
DR   STRING; 1287680.R1GER7; -.
DR   KEGG; npa:UCRNP2_3123; -.
DR   eggNOG; KOG0042; Eukaryota.
DR   HOGENOM; CLU_015740_4_1_1; -.
DR   OMA; PHIVKPM; -.
DR   OrthoDB; 989271at2759; -.
DR   Proteomes; UP000013521; 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; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 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:UP000013521}.
FT   DOMAIN          113..484
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          527..654
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          706..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  79812 MW;  52CB2A7E468FAF07 CRC64;
     MASKGARRFL KPALYSLGAA TVGGGVLYAS LRPREIPGSE AAAVPPPTFG PGGVFNPPNF
     PKVKSRDEQI ADLKSSAARN LSHALDKAKK GFAGLLGSHD SATRDVNGDD PYDLLVIGGG
     ATGTGIALDA ATRGLKVALV ERDDFSSGTS SKSTKLVHGG VRYLEKAVWE LDYSQYKLVV
     EALRERRYFL DTAPHLSQWL PIMIPLDKWW KAPYFWAGTK FYDFLAGSEN IETSYFLTKS
     KALEAFPMLK KTDLVGALVY YDGAHNDSRM NVSLAMTAAL YGATVVNHIE VTGLEKDANG
     RLNGARVKDC IDEANGKVPQ EFTIRAKGII NATGPFTDSI RKMDDQNTKE IVAPSSGVHV
     ILPGYFSPSN MGLIDPSTSD GRVIFFLPWH GNTIAGTTDA PTEVKQNPVA GEQEIDWILN
     EIRGYLAPDI NVRRGDVLAA WSGIRPLVRD PKAKKTEGLV RNHLITVSDS GLLTCAGGKW
     TTYREMSEQT VDEAIKEFGL QVKAVTNPPR VSGTDIVDEK ANLDGTCQTH RVRLIGAHGY
     SKTLFINLIQ HFGIETEVAQ HLCTAYGDRA WTVCSLAEPT EQRYPVRGKR ISPLYPFIDG
     EIRYAVRHEY AQNAVDVIAR RTRLAFLNAQ AALESLPMVI DLMAGELGWD SKRKEREWKD
     AIAFLGSMGL PKGKLALTRK EVEQGKVGKY VDEEYGLYAR HDNPAETLAS DSKFPSGHNP
     VEGSDSPANK
//

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