ID A0A0Q8ECZ7_9ACTN Unreviewed; 506 AA.
AC A0A0Q8ECZ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KRA37668.1};
GN ORFNames=ASD81_02910 {ECO:0000313|EMBL:KRA37668.1};
OS Nocardioides sp. Root614.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA37668.1, ECO:0000313|Proteomes:UP000051699};
RN [1] {ECO:0000313|EMBL:KRA37668.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA37668.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA37668.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA37668.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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:KRA37668.1}.
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DR EMBL; LMGV01000001; KRA37668.1; -; Genomic_DNA.
DR RefSeq; WP_056706581.1; NZ_LMGV01000001.1.
DR AlphaFoldDB; A0A0Q8ECZ7; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000051699; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051699}.
FT DOMAIN 20..376
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 394..495
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 506 AA; 52658 MW; 9F5163A7F42EC923 CRC64;
MTSSPTRLRP GLADAPVSVD LLVIGLGVTG AGVALDAVSR GLSVLAVDAH DLAFGTSRWS
SKLVHGGLRY LANGQVGVAR ESAVERGILM ESTAPHLSHP MPMLLPLMSS VSSAQAALAS
AGFRAGDALR VSAGTSADTL PRPRRISRNE ALRLAPSLRQ QGLRGGLLSW DGQLEDDARF
VTCLARTAAS LGADVRTRAR VLSATGKGAV LRDELTGESV EVSARAVINA TGVWAGSLVE
DVKLKPSRGT HLVVRASTIP GLAAALTVPV PGTTSRFVFA LPQPDGTIYV GLTDEETDGE
IPDVPQGTES EIGFLLDVVG AAFDRPIRRS DVIGTYAGLR PLLDSDGSTA DLSRKHAVLT
SPTGVVTVVG GKLTTYRQMA EDAVDAIGLT QAPCLTRALP LLGAASREEL ALLEAPARLV
RRFGTEAALV LSNAVDVTGL TEDELLAPGP QGVTLAELVF AITHEGAADV DDLLDRRTRV
GLVPEDRAAA LPMAERALAL VPRIVE
//