ID A0A127NV75_9CORY Unreviewed; 570 AA.
AC A0A127NV75;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-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=WM42_1625 {ECO:0000313|EMBL:AMO89345.1};
OS Corynebacterium simulans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=146827 {ECO:0000313|EMBL:AMO89345.1, ECO:0000313|Proteomes:UP000074804};
RN [1] {ECO:0000313|EMBL:AMO89345.1, ECO:0000313|Proteomes:UP000074804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PES1 {ECO:0000313|EMBL:AMO89345.1,
RC ECO:0000313|Proteomes:UP000074804};
RX PubMed=26861018;
RG NISC Comparative Sequencing Program;
RA Tsai Y.C., Conlan S., Deming C., Segre J.A., Kong H.H., Korlach J., Oh J.;
RT "Resolving the Complexity of Human Skin Metagenomes Using Single-Molecule
RT Sequencing.";
RL MBio 7:e01948-15(2016).
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; CP014634; AMO89345.1; -; Genomic_DNA.
DR RefSeq; WP_062036793.1; NZ_CP014634.1.
DR AlphaFoldDB; A0A127NV75; -.
DR STRING; 146827.WM42_1625; -.
DR KEGG; csp:WM42_1625; -.
DR PATRIC; fig|146827.5.peg.1600; -.
DR Proteomes; UP000074804; 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.
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 27..384
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 406..529
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 570 AA; 62078 MW; F5F5A073623D60D5 CRC64;
MTKLSNQSFN PEYFEKAWEN YSDEEYDVVI IGGGSVGAGA AVDAATRGLK TAVVESRDFA
AGTSSRSSKM FHGGLRYLAM FDFRLVAESL HERELNMSTL APHLVKPLKF IFPLTHPVWE
RVMMFGGFTL YDLMGGAKSV PMQKHLTRKG VLNVAPGLKD HAVVGGVRYY DTLVDDARHT
MTVLRTAAEF GASVRTGTEV VGFEKDRGGR IIGAHVRDVA TGREATIKGR VFINATGVWN
DKIQEMAGVE GKFTVHASKG VHIVVPKDAL DADAALCFVT EKSVLFVIPW GEYWIIGTTD
TDWEKGLSLP DPAPTKADID YILDQVNQRV SRTITRSDIV GVYSGLRPLL TGKSDTTTKL
SRNHAVAKVA PGLVSVAGGK YTTYRVIGKD AVDLAVKELT FDAPESVTER TPILGAEGYH
ALANQVPTLA KRYGVHQDVI EHLLGRYGSL LGEVLAPAEE DAELLKPVPG AEQYLWAEVR
YAVTHEGALH LDDILSRRLR IAIEYAHRGV DCADAVANFV APLLGWDDAV KQAEIAAFKQ
HTEAELQAEA ALTDQEANDI LVRAAGKPQV
//
