ID A0A238IYX3_9RHOB Unreviewed; 526 AA.
AC A0A238IYX3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD_1 {ECO:0000313|EMBL:SMX23231.1};
GN ORFNames=BOA8489_01335 {ECO:0000313|EMBL:SMX23231.1};
OS Boseongicola aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Boseongicola.
OX NCBI_TaxID=1470561 {ECO:0000313|EMBL:SMX23231.1, ECO:0000313|Proteomes:UP000201838};
RN [1] {ECO:0000313|EMBL:SMX23231.1, ECO:0000313|Proteomes:UP000201838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8489 {ECO:0000313|EMBL:SMX23231.1,
RC ECO:0000313|Proteomes:UP000201838};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; FXXQ01000003; SMX23231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238IYX3; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000201838; 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:UP000201838}.
FT DOMAIN 7..384
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 406..502
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 526 AA; 58615 MW; B53553D09E614382 CRC64;
MADRAVDLFI IGGGINGTGI ARDAQGRGLQ VKLAEMNDLA SATSSASTKL FHGGLRYLEY
FEIELVKKAL VERETLLKAM PHISWPMRFV LPYHKDMRFE NSTPASKLLN IFMPWMRGRR
PGWMIRLGLY AYDNLGGREI LPGTKTVNLK RDPAGAALDD KFEKAYEYSD CWVEDARLVA
LNARDAAERG ATILVRTRVL TAEREGDLWR IETLDLMTGG RHTHLARAIV NAGGPWVEDI
VRGVARLNTS EGVRLVKGSH IVTKRLFDHD KSYFFQGEDG RIIFAIPYET DFTLIGTTDQ
EYEGDPSKAT CSAAEADYLI NFVNRYFKND ISRKDIIWTY SGVRPLYDDG AKSATAATRD
YVLSLDENGP PILSVFGGKI TTYRKLAEQA MAKLEPFFTY SKGDWTAGVA LPGGDFAVAD
FDALVARVLT DFPFLTPFWA RRLVRAYGTD AWMVLGSAAS ADDLGEDFGA TLTDAEVKWL
VSKEYARSAE DIVWRRSKLG LRLTPAQIAR LDETMPQPLV VSASKN
//
