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Database: UniProt
Entry: H0R0P4_9ACTN
LinkDB: H0R0P4_9ACTN
Original site: H0R0P4_9ACTN 
ID   H0R0P4_9ACTN            Unreviewed;       580 AA.
AC   H0R0P4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
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:GAB18645.1};
GN   ORFNames=GOEFS_060_00380 {ECO:0000313|EMBL:GAB18645.1};
OS   Gordonia effusa NBRC 100432.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB18645.1, ECO:0000313|Proteomes:UP000035034};
RN   [1] {ECO:0000313|EMBL:GAB18645.1, ECO:0000313|Proteomes:UP000035034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB18645.1,
RC   ECO:0000313|Proteomes:UP000035034};
RA   Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL   Submitted (DEC-2011) 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:GAB18645.1}.
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DR   EMBL; BAEH01000060; GAB18645.1; -; Genomic_DNA.
DR   RefSeq; WP_007317981.1; NZ_BAEH01000060.1.
DR   AlphaFoldDB; H0R0P4; -.
DR   STRING; 1077974.GOEFS_060_00380; -.
DR   eggNOG; COG0578; Bacteria.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000035034; 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; 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:UP000035034}.
FT   DOMAIN          31..385
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          407..531
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   580 AA;  63933 MW;  DF8F16BB8D20898C CRC64;
     METDFNPDRP ADLGPAQRVE AWRRLSEEQF DILVVGGGIV GVGAALDAAT RGLRVALVEA
     RDIASGTSSR SSKMFHGGLR YLEQLEFGLV REALHERELS LTLLAPHLVK PLPFLYPLTQ
     RFWERPYVSA GLFLYDRMGG AKSVPGQRHV SRLGALRVAP ALKRNSLVGG IRYYDTVVDD
     ARHSLTVART AAQYGAVVRT STQVVGFLKE ADRVLGAKVR DTETGETTEI RAHCVINAAG
     VWTDEVQALS KQRGHFRVRA SKGVHIVVPR DRIVSETAII LRTTKSVLFV IPWETHWIIG
     TTDTDWNLDL AHPAATRADI DYILDRVNEV LVSPLTHNDI EGVYAGLRPL LAGEDDDTSS
     LSREHAVAAV APGLISIAGG KYTTYRVMAA DAVDACNDYI PTRVAPSITQ RVPLLGADGY
     FALINQCEHL GHRFGLHPYR IRRLLNRYGS LVDDVLYYAD DDPSLLKPLA AAPQYLRAEF
     VYAARNEGAL HLEDLLARRT RIAIEYNHRG VDCAAEVAEL VAPILGWDTQ RTAFEVANYV
     ARVEAEIASQ RQPDDLSADA LRAAAPESRR EILEPVPVPE
//
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