ID A0A2A2SKH7_9SPHN Unreviewed; 485 AA.
AC A0A2A2SKH7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:PAX09733.1};
GN ORFNames=CKY28_03110 {ECO:0000313|EMBL:PAX09733.1};
OS Sphingomonas lenta.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1141887 {ECO:0000313|EMBL:PAX09733.1, ECO:0000313|Proteomes:UP000218151};
RN [1] {ECO:0000313|Proteomes:UP000218151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1PNM-20 {ECO:0000313|Proteomes:UP000218151};
RA Feng G., Zhu H.;
RL Submitted (SEP-2017) 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:PAX09733.1}.
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DR EMBL; NSLI01000001; PAX09733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2SKH7; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000218151; 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: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:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 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.
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:UP000218151}.
FT DOMAIN 4..349
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 372..466
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 485 AA; 53780 MW; 4A2764D7B72E630F CRC64;
MTYDLLIVGG GINGCAIARE AALNGWSVLL VERDDLASHT SSASTKLIHG GLRYLEYYDF
RLVAHALRER ERLLRLAPHL IRPLTFVLPH ENAVRPWWLV RLGLLLYDRL GGRSALPRSR
GLRRSDAAYR APLKNAGSGF VYSDAWVDDS RLTVLNALDA AEHGAEVLTR TTLESARRED
GLWRARLSDG REVQARAVVN AAGPWVAELL GRMGVNASAG VRLVKGSHIV VPRLFEGDHA
YILQQPDRRI VFAISYEGGT AVGTTDVVVE RPEDARIDGD EVRYLCDAAS RYFARQVGPE
DVTSSWSGVR PLYDDGASEA REVTRDYVLE LDANGPPLLS VFGGKITTAR HLAEEAVAKV
APALGRHVEP MTRERPFPGG GFRSFDAYLA HVRERRPWLG AERSERMARA YGTLLVAMLA
GVRDEAGMGE AFGAGLTERE VRWMRDREWA RTPEDVLERR SKLGLHMTAA ERVRFEAWWA
ASPAA
//
