ID H5U4U4_9ACTN Unreviewed; 580 AA.
AC H5U4U4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:GAB40752.1};
GN ORFNames=GOSPT_115_00090 {ECO:0000313|EMBL:GAB40752.1};
OS Gordonia sputi NBRC 100414.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB40752.1, ECO:0000313|Proteomes:UP000005845};
RN [1] {ECO:0000313|EMBL:GAB40752.1, ECO:0000313|Proteomes:UP000005845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB40752.1,
RC ECO:0000313|Proteomes:UP000005845};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sputi NBRC 100414.";
RL Submitted (FEB-2012) 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:GAB40752.1}.
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DR EMBL; BAFC01000113; GAB40752.1; -; Genomic_DNA.
DR RefSeq; WP_005207840.1; NZ_BAFC01000113.1.
DR AlphaFoldDB; H5U4U4; -.
DR eggNOG; COG0578; Bacteria.
DR Proteomes; UP000005845; 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}.
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"
FT REGION 547..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 63721 MW; 5EF38E27DEE17243 CRC64;
METEFNPDRP ADLGPLYREQ AWRRLGTEQF DIVVIGGGVV GVGAALDAAT RGLRVALVEA
RDIASGTSSR SSKMFHGGLR YLEQLEFGLV REALHERELS LSLLAPHLVK PLPFLYPLTH
RVWERPYVAA GIFLYDTMGG AKSVPGQKHV TRSGALRVAP ALKRDSLIGG IRYYDTVVDD
ARHSLTVGRT AANYGAVIRT STQVVGFLRD ADRIMGVRVR DTENGETAEI KAHCVINAAG
VWTDEVRALS KQRGRFKVRA SKGVHIVVPR DRIVSETAII LRTASSVLFV IPWETHWIVG
TTDTDWHLDL AHPAATRADI DYLLERVNEV LVTPLRHDDI EGVYAGLRPL LAGEDEATSK
LSREHAVAEI APGLISIAGG KYTTYRVMAA DAVDACVDFI PTRVAPSITE RVPLIGADGY
FALINQCESL GEKYGLHPYR IRRLLNRYGS LIDDVLFYAA DDPSLLRPLE AAPQYLRVEV
VYAAVDEAAL HLEDILARRT RISIEYAHRG VDCAQEVADL VAPVLGWGPE KVAFEVETYK
ARVAAEIASQ QQPDDESADA LRAAAPESRV DILEPVPIPD
//
