ID A0A1P8UAE9_9MICO Unreviewed; 583 AA.
AC A0A1P8UAE9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:APZ35097.1};
GN ORFNames=BOH66_13210 {ECO:0000313|EMBL:APZ35097.1};
OS Microbacterium aurum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=36805 {ECO:0000313|EMBL:APZ35097.1, ECO:0000313|Proteomes:UP000187185};
RN [1] {ECO:0000313|EMBL:APZ35097.1, ECO:0000313|Proteomes:UP000187185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 15219 {ECO:0000313|EMBL:APZ35097.1,
RC ECO:0000313|Proteomes:UP000187185};
RA Jung Y., Shin J.-H., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "Complete genome sequence of Microbacterium aurum KACC 15219.";
RL Submitted (DEC-2016) 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 ---------------------------------------------------------------------------
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; CP018762; APZ35097.1; -; Genomic_DNA.
DR RefSeq; WP_076691476.1; NZ_JAFBCQ010000001.1.
DR AlphaFoldDB; A0A1P8UAE9; -.
DR STRING; 36805.BOH66_13210; -.
DR KEGG; maur:BOH66_13210; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000187185; Chromosome.
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: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:UP000187185}.
FT DOMAIN 19..367
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 427..546
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 564..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 62175 MW; 813BF272E810CDA2 CRC64;
MTDTARRTTQ TLAERPYADV LIIGGGINGL ATLRDLALQG VDVALVERGD FVSGASAASS
HMIHGGIRYL ENGEFRLVHE AVTERNALLK TAPHYVRPLQ TTIPIYSTFS GVLSAPLRFL
RHSAGQHRER GAALIKIGLV IYDSFSRGGG LLGKGTVPRH AFHGRKRSLE QLPQLNPGVR
YTATYWDASL RDPERLALDV LRDGLAAGGD RARAANYTEA VGADGGKVTL RDGVTGEEFA
FTASVVVNAS GPWTDLTNLA LGDPTHYMGG TKGSHIVLEH EELLAATGGC ELFFEHSDGR
IVLIYPLKGR VLVGTTDLEH DMREPIVCTE AEIDYFFELI AHVFPGIAVD RSQIVYRFAG
VRPLPGHGDL APGFVSRDYR IEAERLPGAD APTVLSLVGG KWTTFRASAA HLTDRVLELL
ARPRLRSTKG LPIGGGAGFP TSERARRQWV AAHADRVGFD RAAVLLDRYG TGAAEVIAAI
GDDDTPLRTV PSYSRDELRH LAATELVVHL ADVLLRRTAI AFLGAATREA AVEVAEVIAP
VLGWDAGAQA AEVDQALAAV HAADPASGPA TAPADAGAPS PAR
//
