ID A0A0Q8CKC5_9MICO Unreviewed; 585 AA.
AC A0A0Q8CKC5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KRA10629.1};
GN ORFNames=ASD61_00185 {ECO:0000313|EMBL:KRA10629.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA10629.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA10629.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA10629.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA10629.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA10629.1,
RC ECO:0000313|Proteomes:UP000051073};
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:KRA10629.1}.
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DR EMBL; LMGR01000001; KRA10629.1; -; Genomic_DNA.
DR RefSeq; WP_055817254.1; NZ_LMGR01000001.1.
DR AlphaFoldDB; A0A0Q8CKC5; -.
DR STRING; 1736567.ASD61_00185; -.
DR Proteomes; UP000051073; 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:UP000051073}.
FT DOMAIN 31..373
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 434..558
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 585 AA; 62691 MW; 53B5D5529E81641E CRC64;
MATSSTTSTS SSGADALRPA VEALRARPHA DVLVIGAGIN GIATFRDLAL QGVDVVIIDR
DDYVSGASAA SSHMIHGGIR YLENGEFRLV RESVEERNAL VRIAPHYVRP LKTTVPIFST
FSGILSAPLR FLTHKAGKPT ERGAALIKVG LTAYDSFSRD GGSVPRHEFH GRKRSLAELP
ALNPGIKYTA TYYDASMHDP ERLALDVLSD GLAAGPHARA ANYVEAAGAD GDAITLRDTV
TGEEFGFTAS VVVNASGPWT DLTNEALGGA TRFMGGTKGS HIVLDHPELL AATDGREIFF
EHEDGRIVLI YPLKGRVLVG TTDLEHDMRK PIRTTEDEVD YFFDLISHVF PGIAVNRSHI
VYRFAGVRPL PRHDETQPGF VSRDYRIEET TVPGSGGAVP LLSLVGGKWT TFRALAEHLG
DEVLAKLGRA RTTSTEGLAI GGGRGYPTTD AARTVWLASQ GEVLGRARAE ELLERYGTRA
ESLIADLAES GTDVPLASAP AYSVGEIAAL AREEQVVHLI DVLKRRTSLA FVGAVTADVL
SELADVVGDA LGWTGARRAA EIEHARIELH DAHGVAIEER RTAHA
//
