ID A0A167AUH5_9PEZI Unreviewed; 759 AA.
AC A0A167AUH5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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};
DE Flags: Fragment;
GN ORFNames=CI238_12625 {ECO:0000313|EMBL:KZL80537.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL80537.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL80537.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL80537.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL80537.1}.
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DR EMBL; LFIW01001886; KZL80537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167AUH5; -.
DR STRING; 1573173.A0A167AUH5; -.
DR Proteomes; UP000076584; 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.
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:UP000076584}.
FT DOMAIN 164..531
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 571..688
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL80537.1"
SQ SEQUENCE 759 AA; 82029 MW; 8C028CB16D36CCCF CRC64;
LSFLFSAVPF YSLFPPSPPL PLLPRIIICD PPSKQTNTEE EHLQISHHAP GTVDLRTAQR
HTRPFWTRCK SPPSEEKRPI HSMASRFSSL RRPVAIAAAA ATGGVVAYST FLGGRGAHSF
DKPLVELKRD NQGKIVPPSF PSTKDRASQL ADLRAHNSDN DEYDLLVIGG GATGTGIALD
AVTRGLKVAL VERDDFSAGT SSKSTKVVHG GVRYLEKAVW NLDYSQLELV MEALHERKTF
LNVAPHLSSS LPILLPIQKW WQTPYFWAGT KAYDLLAGSQ GLESSYYVST NKALEAFPML
RRDNMVGALV YYDGQHNDSR MNISLALTAA LYGATVINHV EVTSLEKNSN GKIVGAKVRD
VMTPGSNSFT VRAKGVINAT GPFADAVERM DNPDRKPIVA PASGAHIMLP GDICPNGIGL
LDAATSDGRV IFVLPWQGYT LAGTTDNAAP VEREPIARED DIKFILKEVN KLITPESALS
RSDVLAAWSG IRPLVKDPNA KNTESLVRSH LVTVSDSGLL TCAGGKWTTY RQMAEDAVDE
AIKTFKLQPK PVALPDISGA GLPTFTTTGQ CITTNVPLIG AHGFSKHLPG HLISQFSLDV
DIANHLAHNY GDRAWSVAAD SSERIIPNFP FVVGEIRHGV RAEAAMTATD LISRRTRLAF
LDAESALRAL PRVIDVMAEE LGWNEARKNK EWTETVHFLQ SMGLSADKLN VTREEVLSSG
GTKSGYAPKA QIAASASGFK TGLGDIQAGG ALARNITEA
//
