ID A0A0N0T996_9ACTN Unreviewed; 568 AA.
AC A0A0N0T996;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KOV85975.1};
GN ORFNames=ADL01_07440 {ECO:0000313|EMBL:KOV85975.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV85975.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV85975.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV85975.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-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:KOV85975.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGDW01000051; KOV85975.1; -; Genomic_DNA.
DR RefSeq; WP_053741098.1; NZ_LGDW01000051.1.
DR AlphaFoldDB; A0A0N0T996; -.
DR PATRIC; fig|1519490.3.peg.1624; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000037738; 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.
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:UP000037738}.
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 539..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 61952 MW; 7EE98D3EA8BA0E6B CRC64;
MRTAALGPAQ RAESLAAMAE RELDVLVVGA GVVGAGTALD SVTRGLSTGL VEARDWASGT
SSRSSKLIHG GLRYLEMLDF ALVREALKER GLLLERLAPH LVKPVAFLYP LQHQGWERLY
AGAGVALYDA MSMARGHGRG LPAHRHLSRR HALRVAPALK KDALVGALQY YDAQMDDARY
VATLVRTAAA YGAKVANRAR VTSFLREGER VVGARVQDVE GGGEYEIRAR QIVNATGVWT
DDTQAMVGQR GQFHVRASKG IHLVVPKDRI HSTTGLILRT EKSVLFVIPW GRHWIVGTTD
TDWDLDKAHP AASSADIDYL LEHVNSVLAV PLTRDDVQGV YAGLRPLLAG ESDATSKLSR
EHTVAHPVPG LVVVAGGKYT TYRVMAKDAV DAAVHGLDQR VAECVTEDVP LLGAEGYRAL
WNARARTAAR TGLHVVRVEH LLNRYGSLAQ EVLDLIAADS SLGEPLQAAD DYLRAEIVYA
ASHEGARHLD DVLTRRTRIS IETFDRGTRS SREAAELMAP VLGWDKDQIE REVEHYDKRV
EAERESQRQP DDLTADAARL GAPDIAPL
//