ID A0A1B1ZQI9_9PSEU Unreviewed; 570 AA.
AC A0A1B1ZQI9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=AFB00_19065 {ECO:0000313|EMBL:ANY08041.1};
OS Pseudonocardia sp. HH130630-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1690815 {ECO:0000313|EMBL:ANY08041.1, ECO:0000313|Proteomes:UP000092926};
RN [1] {ECO:0000313|EMBL:ANY08041.1, ECO:0000313|Proteomes:UP000092926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130630-07 {ECO:0000313|EMBL:ANY08041.1,
RC ECO:0000313|Proteomes:UP000092926};
RA Oliw E.H.;
RL Submitted (JAN-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}.
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DR EMBL; CP013854; ANY08041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1ZQI9; -.
DR STRING; 1690815.AFB00_19065; -.
DR KEGG; phh:AFB00_19065; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000092926; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092926}.
FT DOMAIN 24..377
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..528
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 540..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 61314 MW; 95CEE187B46D7E8B CRC64;
MKSVALSPEA RTAALQAMGD RELDVLVVGG GVVGAGSALD AATRGLSVGL VEARDFASGT
SSRSSKLVHG GLRYLEMLDF RLVAEALAER GLLIQQLAPH LVRPVPFLYP LQHRGWERLY
AGAGVALYDT LGFLSGRSRG VPHHRHLTRR GARRVVPSLR KDALVGALQY YDAQVDDARH
TMFIARTAAA YGAHVATRAR VVGLLKEAGR VVGATVQDLE SGEQVDVRAK QVINATGVWT
DDTQGLAGER GLFKVRASKG IHLVVPRDRI RGESGLILRT EKSVLFVIPW GRHWIIGTTD
TGWDLDKAHP AASAADIDYL LQHVNTVLEQ PLTHDDVEGV YAGLRPLLSG ESESTSKLSR
EHAVATPVPG LVVVAGGKYT TYRVMAKDAV DAAVHGLDAK VPASCTAEVP LLGAEGYHAL
TNATANLARS SGLHPARIEH LLGRYGSLIQ EVLDLAAADP TLTEPLAGAP DYLRAEVVYA
ASHESARHLE DILARRTRIS IETFDRGVEA TQEAARLVAP VLGWNDEQVE REVDHYRKRV
EAERESQRMP DDATADAARL GAPDVVPVSG
//
