ID A0A0F2C7K8_9MICO Unreviewed; 489 AA.
AC A0A0F2C7K8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD_1 {ECO:0000313|EMBL:KJQ54698.1};
GN ORFNames=RS85_01428 {ECO:0000313|EMBL:KJQ54698.1};
OS Microbacterium sp. SA39.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ54698.1, ECO:0000313|Proteomes:UP000033425};
RN [1] {ECO:0000313|EMBL:KJQ54698.1, ECO:0000313|Proteomes:UP000033425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA39 {ECO:0000313|EMBL:KJQ54698.1,
RC ECO:0000313|Proteomes:UP000033425};
RA Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (JAN-2015) 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:KJQ54698.1}.
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DR EMBL; JXRU01000031; KJQ54698.1; -; Genomic_DNA.
DR RefSeq; WP_046012738.1; NZ_JXRU01000031.1.
DR AlphaFoldDB; A0A0F2C7K8; -.
DR STRING; 1263625.RS85_01428; -.
DR PATRIC; fig|1263625.4.peg.1438; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000033425; 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: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:UP000033425}.
FT DOMAIN 26..384
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 425..473
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 489 AA; 51900 MW; E1E25F0C0111EC7B CRC64;
MIPSSSDLDA RRRRRELEDA AVDTTDVLVV GGGITGVGVA LDAASRGLAV TLIEAEDLAF
GTSRFSSKLV HGGLRYLATG DVATARESAR ERHLLMTVIA PHLIRPLPQL LPFRPGVTWR
QRGAGAVGMT LGDLLRVEAR TPRSVLPAPR PVSARTAQRL FPALDARGLR GGMLSYDGQL
VDDARLVVAV ARTAAGMGAR ILTRVRAEEL RADGASAVDA LTGERFYIRA RSVINATGVW
AGTLDEAIAV RPSRGTHIVL DAADLGHPTA ALTVPHEGSI SRYVFALPQR GGRVIVGLTD
EDAPGPVPRV AQATEPEVDF LLSTLNRVVT RPLTRAQVRG AFAGLRPLID NGADATADVS
RRHLVASADA GFINVLGGKL TTYRRMAEDA VDLAVRVRAL DAAPSRSSSL RLIDDHAADR
AEFADAGDAV AEGIAVTRAE IEFAVRAEGA LTAEDVLDRR TRIGLVDADR ERSQVAVETI
VAWTLAEIG
//
