ID L0A3I1_DEIPD Unreviewed; 531 AA.
AC L0A3I1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:AFZ67994.1};
GN OrderedLocusNames=Deipe_2529 {ECO:0000313|EMBL:AFZ67994.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ67994.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) 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}.
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DR EMBL; CP003382; AFZ67994.1; -; Genomic_DNA.
DR RefSeq; WP_015236296.1; NC_019793.1.
DR AlphaFoldDB; L0A3I1; -.
DR STRING; 937777.Deipe_2529; -.
DR KEGG; dpd:Deipe_2529; -.
DR PATRIC; fig|937777.3.peg.2535; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_4_1_0; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000010467; 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:UP000010467}.
FT DOMAIN 21..379
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 410..500
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 531 AA; 57694 MW; F4B7DC8BE613734C CRC64;
MSTINPRSTF LEQLRTTPIW DIVIIGGGAS GLGAAVEAAS RGYKTLLLEA HDFAKGTSSR
STKLVHGGVR YLAQGNIGLV REALRERGLM RKNAPHLVHD MSFVVPAYDW WAGPFYGVGL
KMYDLLAGKL NLGGSKYLGK EETLRHTPTL QGEGLRGGIL YHDGQFDDAR LAVTLMRTVL
DHGGVTLNYL PVTGLLKEEG KVCGATARDS ESGQEFTVRA RAVVNATGVF VDQIRRMDEP
GARDMLSPSQ GVHVVVDKRF LPGDSAIMIP RTEDGRVLFA VPWHDHVVIG TTDTAVPHAS
LEPRALPEEI EFILRTAGQY MNPAPTRADV KSVYVGLRPL VKAETSDGVG STAQLSRDHV
LRVAPSGLIT LTGGKWTTYR HMGEDAIDRA AEVGALPTRL SLTQGLRLHG WTETPEAAPL
DVYGTDAAHL RQLAGAETAL HPELPYLEAE VRWAARCELA RTVEDVLSRR TRALLLNARA
SEQAALRVAQ LLAEELGHDA HWIATQVAQF RELARGYQLD AVAEPDLSAS S
//
