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Database: UniProt
Entry: E6SCV2_INTC7
LinkDB: E6SCV2_INTC7
Original site: E6SCV2_INTC7 
ID   E6SCV2_INTC7            Unreviewed;       512 AA.
AC   E6SCV2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=Intca_0983 {ECO:0000313|EMBL:ADU47507.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS   12989 / 7 KIP).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU47507.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU47507.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA   Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
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; CP002343; ADU47507.1; -; Genomic_DNA.
DR   RefSeq; WP_013491825.1; NC_014830.1.
DR   AlphaFoldDB; E6SCV2; -.
DR   STRING; 710696.Intca_0983; -.
DR   KEGG; ica:Intca_0983; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000008914; 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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 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:UP000008914}.
FT   DOMAIN          24..356
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          402..508
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   512 AA;  53949 MW;  323505B0449B3B71 CRC64;
     MTAPAIDRRA RARALESLAT SRYDCIVVGG GVTGAGVALD AASRGLRTAL IERVDLAAGT
     SRWSSKLVHG GLRYLAKGDV GIAWESARER HALMTTIAPH LTRAAANIVP LDGSTPPPLG
     LLTEAGIRLA DGLRLASHTS RHLLPRPSRI SASEALVMAP GLRQDGLRGG LLFWDGQLED
     DARLGTAIAR TAVAHGADVV TRCAATELTD TTVTLRDELA GESFTAHGHV VNATGVWAGE
     HEPSVHIKPS RGSHVVVRSE AVGRPRAIFT APVPGHFGRF VFAMPQSDGL VIIGLTDEPV
     GDVDGVAPEV PCADTRFLLD TINQVLEQPL AESDVVGRYA GLRPLVTTAA DGPTADVSRR
     HLLVDEPGGP VTITGGKLTT YRQMAEATVD AVCRRVRSPA SCRTRSLPLV GAASREVLSR
     VPAPERLVRR YGTEATDVAA LGLAHPELMR PVSDSCPTLG VELLFGVLHE GALTAADLVE
     RRTRISFDAQ AVDAAREVAD RVLALAADLA RA
//
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