ID A0A1A2B7L3_9MYCO Unreviewed; 585 AA.
AC A0A1A2B7L3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=A5753_11030 {ECO:0000313|EMBL:OBF64397.1};
OS Mycobacterium sp. 852002-51971_SCH5477799-a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834106 {ECO:0000313|EMBL:OBF64397.1, ECO:0000313|Proteomes:UP000091887};
RN [1] {ECO:0000313|EMBL:OBF64397.1, ECO:0000313|Proteomes:UP000091887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852002-51971_SCH5477799-a {ECO:0000313|EMBL:OBF64397.1,
RC ECO:0000313|Proteomes:UP000091887};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:OBF64397.1}.
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DR EMBL; LZIF01000087; OBF64397.1; -; Genomic_DNA.
DR RefSeq; WP_067128428.1; NZ_LZIF01000087.1.
DR AlphaFoldDB; A0A1A2B7L3; -.
DR STRING; 1834106.A5753_11030; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000091887; 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 37..391
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 413..537
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 585 AA; 63243 MW; 99B4FE14B59A9CF0 CRC64;
MSNPIQAPDS LQTWAASSLG PRQRALAWER LGAEQFDVVV IGGGVVGSGC ALDAATRGLK
VALVEARDFA SGTSSRSSKM FHGGLRYLEQ LEFGLVREAL YERELSLTTL APHLVKPLPF
LFPLTKRLWE RPYVAAGIFL YDSLGGAKSV PAQKHLTRAG ALRLSPGLKR SSLVGGIRYY
DTVVDDARHT MTVARTAGHY GAVVRTSTQV VAMLREGDRV TGVRVRDSED GAITEVRGHV
VVNATGVWTD EIQALSKQRG RFQVRASKGV HVVVPRDRVV SDVAIILRTE KSVMFVIPWG
SHWIIGTTDT DWNLDLAHPA ATKADIDYIL ETVNTVLAIP LTHADIDGVY AGLRPLLAGE
SEETSKLSRE HAVAVPAPGL VAIAGGKYTT YRVMAADAVD AAAQFIPARV APSITEKVSL
LGADGYFALI NQAEHVAQLQ GLHPYRVRHL LDRYGSLIGD VLALAAQSPD LLEPIKEAPG
YLRVEALYAV TAEGALHLED ILARRMRISI EYPHRGVDCA REVADVVAPI LGWSAEEVAR
EVANYTARVE AEILSQAQPD DVSADELRAS APEARAEILE PVPLS
//
