ID M3HSA6_LEPBO Unreviewed; 549 AA.
AC M3HSA6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:EMG00941.1};
GN ORFNames=LEP1GSC123_3300 {ECO:0000313|EMBL:EMG00941.1};
OS Leptospira borgpetersenii str. 200701203.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMG00941.1, ECO:0000313|Proteomes:UP000011783};
RN [1] {ECO:0000313|EMBL:EMG00941.1, ECO:0000313|Proteomes:UP000011783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701203 {ECO:0000313|EMBL:EMG00941.1,
RC ECO:0000313|Proteomes:UP000011783};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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:EMG00941.1}.
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DR EMBL; AKWO02000039; EMG00941.1; -; Genomic_DNA.
DR AlphaFoldDB; M3HSA6; -.
DR BioCyc; LBOR1193007:G11KN-2447-MONOMER; -.
DR Proteomes; UP000011783; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011783};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..388
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 430..534
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 549 AA; 62392 MW; E55988C8A41AC589 CRC64;
MSKNKKSPSN TRSAKSQDSF VYDLLVIGGG ITGAHVLWDS TLRGMKSILL EKNDYASGTS
QATSKMIHGG LRYLKNFELG LVRESLRERA ILARITPQAV QTMGFLVPIY SNIERLVLKV
GMEMYNALSY DRNANISQDR SIPKYSFLSK EQTTMESPTI ERDKLKGSYL YYDYLNINPE
RHTCEFIFSA RERGAEAKNY TEVTSITRST DSLYTVVARD KISGKEISFQ TKSVVNATGP
WADLVESLAG VEIEKHLVRS KGIHIVTRKI CGDKTLVTKK KDGTHLFIIP WRNKTIIGTT
DTEYINSPDR FRVTKKDIEE LLSEINYSFG YTNLTLNDVD FYYGGLRPLV EDPGEPKSTY
NTSRKTEIFD HKESGFPGFF TAMGGKYTTS RSVGEAVVNK VADYLPGNFS ACETSVTPPS
TGNYLDLLSF IKELAKKFPK LSGESIETIA FRYGLQAYQI LEKSSSREEF YTLQNGEKFF
ESEVRFIANR EDIRFATDFF FRRSGVGVPG LPEEKETTKL VRSLAKYLRW NQNRISKEIK
AVKERYRIY
//
