ID A0A1I6FQN2_9RHOB Unreviewed; 533 AA.
AC A0A1I6FQN2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN04488005_0265 {ECO:0000313|EMBL:SFR32198.1};
OS Yoonia tamlensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=390270 {ECO:0000313|EMBL:SFR32198.1, ECO:0000313|Proteomes:UP000199478};
RN [1] {ECO:0000313|Proteomes:UP000199478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26879 {ECO:0000313|Proteomes:UP000199478};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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DR EMBL; FOYP01000001; SFR32198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6FQN2; -.
DR STRING; 390270.SAMN04488005_0265; -.
DR Proteomes; UP000199478; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.250.1890; -; 1.
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.
DR PROSITE; PS00977; FAD_G3PDH_1; 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 ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000199478}.
FT DOMAIN 12..388
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 410..511
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 533 AA; 59294 MW; 49C9CA15BB007F81 CRC64;
MSALSPSDET CDLFIIGGGI NGCGIARDAA GRGLNVRLAE MSDLASATSS ASTKLFHGGL
RYLEYFEVRL VREALIERET LLRAMPHISW PMRFVLPYHK DMRFEGSTPA SKILNTVMPW
MRGRRPAWLI RFGLFLYDNL GGRKILPPTS TVDLRNSPEG APLNDKFTKA YEYSDCWVED
SRLVALNARD AALRGAQIMI RTKVTNAERV GDIWEITTED YAGATKTHRA RMLINAAGPW
VGDVIHNKIG VDSTEDVRLV RGSHIVTPKL YDHDKCYFFQ GTDGRIIFSI PYENDFTLIG
TTDADHSDPD QRPTCTEAER DYLINFANGY FKTPISADDV VWSYSGVRPL YDDGATSATA
ATRDYTLKVD ADGAPILNIF GGKITTYRRL AESALEKVQT YFPETGSKWT AGVPLPGGDF
EVADFDKKVS DLATTYPFLT PAHARRLVRA YGTDAVKMIG DATSLDDLGP HFGADLYAKE
ISWLITHEFA RTAEDIVWRR SKLGLRLSPD EIAALDAWMQ TLLRAQTNDD TAN
//
