ID C1B378_RHOOB Unreviewed; 514 AA.
AC C1B378;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:BAH54995.1};
GN OrderedLocusNames=ROP_67480 {ECO:0000313|EMBL:BAH54995.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH54995.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH54995.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH54995.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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}.
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DR EMBL; AP011115; BAH54995.1; -; Genomic_DNA.
DR RefSeq; WP_015890431.1; NC_012522.1.
DR AlphaFoldDB; C1B378; -.
DR STRING; 632772.ROP_67480; -.
DR KEGG; rop:ROP_67480; -.
DR PATRIC; fig|632772.20.peg.7035; -.
DR HOGENOM; CLU_015740_5_1_11; -.
DR OMA; GVMTIMN; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000002212; Chromosome.
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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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 Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 34..360
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 413..506
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 53710 MW; 7636F8811C9B06D4 CRC64;
MTHPSTPSVS RSSALNSARR TRELDQLSDG ARVDVLVIGG GVTGVGVALD AASRGLDVVL
VEKRDLAFGT SRWSSKLAHG GLRYLASGNV GIARESAVER GILMTRTAPH LVRALPQLVP
VLDSTTLLGK SLVRTGFLAG DLLRASARTP SAVLPRSRTV RADRVVELAP AVRRDGLRGG
LMAFDGQLVD DARLVVSLAR TAALHGAKVL TRTGAYDVTA TSATLRDELT GSELSIRARA
VVNAAGVWAG EIDPSITLRP SRGTHLVLPA ERLGNPAAAL TVPIPGETNR FVFALPAQLG
RVYLGLTDEA APGPVPDVPE ASEQEIDFLL DTVNTALEVP LRRSDVLGTF AGLRPLLDTG
DGSTADLSRN HAVLRSDTGP VSVVGGKLTT YRKMAEDAVD AAVAAAGLDA RPCRTRALPL
VGAATPEALR NVSAPQALLA RYGTEAALIA AADPALLAPI AEGVDVSRAE LEFAVTHEGA
LDVDDLLDRR TRIGLVPADR ARSLAAAEAV FEKR
//