GPD_COLGL
ID GPD_COLGL Reviewed; 420 AA.
AC Q7Z8E7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)];
DE EC=1.1.1.8;
OS Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=474922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14563847; DOI=10.1074/jbc.m308363200;
RA Wei Y., Shen W., Dauk M., Wang F., Selvaraj G., Zou J.;
RT "Targeted gene disruption of glycerol-3-phosphate dehydrogenase in
RT Colletotrichum gloeosporioides reveals evidence that glycerol is a
RT significant transferred nutrient from host plant to fungal pathogen.";
RL J. Biol. Chem. 279:429-435(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8;
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AY331190; AAP94992.1; -; mRNA.
DR AlphaFoldDB; Q7Z8E7; -.
DR SMR; Q7Z8E7; -.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase.
FT CHAIN 1..420
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)]"
FT /id="PRO_0000138089"
FT REGION 190..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 16..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 344..345
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 373
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
SQ SEQUENCE 420 AA; 45278 MW; ECCB6A3D3D1DF128 CRC64;
MASLGADKKH KVTVVGSGNW GSTICKIVAE NTKANPDLFE EAVHMWVFEE DVVIDKSSPY
YDPAVGDAPQ KLTGVINKYH ENTKYLPGIK LPDNIIANPS LQDAVKDSTI LVFNLPHQFI
GNVCKQLRGH IMPFARGISC IKGVNVSDDG ISLFSEWIGD GLGIYCGALS GANIASEIAA
EKWSETTIAY DPPPMDNSRA PTPRSNSPAN GNGIAPLTPV EMQHKDARGR TSKTKLTPVP
AEYPPLDHQI FKQLFHRPYF HVRMVSDVAG VSLGGALKNI VALAAGFVDG RGWGDNAKAA
IMRVGLLEMV NFGKEFFGQT VHTGTFTEES AGVADLITSC SGGRNFRCAK MAVAEGLSVE
EIEKRELNGQ LLQGTSTAKE VNSFLKARGL EKDYPLFTAV HGILEGRHSV DDIPSLVSDS