ID A0A0B4CZM3_9RHOB Unreviewed; 511 AA.
AC A0A0B4CZM3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=RA29_18435 {ECO:0000313|EMBL:KIC47903.1};
OS Tateyamaria sp. ANG-S1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tateyamaria.
OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC47903.1, ECO:0000313|Proteomes:UP000031171};
RN [1] {ECO:0000313|Proteomes:UP000031171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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}.
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:KIC47903.1}.
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; JWLL01000010; KIC47903.1; -; Genomic_DNA.
DR RefSeq; WP_039688933.1; NZ_JWLL01000010.1.
DR AlphaFoldDB; A0A0B4CZM3; -.
DR STRING; 1577905.RA29_18435; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000031171; 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; 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:UP000031171}.
FT DOMAIN 8..380
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 397..503
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 511 AA; 56238 MW; 3EF79888711AB101 CRC64;
MADEKVFDLF VIGGGINGAG IARDASGRGL SVAMAEAGDL GGATSSASTK LFHGGLRYLE
FFEFGLVKSA LKEREVLLKA MPHISWPMRF VLPYAPDMRF DSDTPTSRLL RVTMPWIEKG
RRPAWLVRLG LFLYDNLGGR EILPGTKTLD LTKAPEGAGL KSRFKMAYEY SDAWVEDSRL
VMLNARDAEA RGATILTRCA VKEAARDGDT WRIETEKGTF RAKALVNAGG PWVADILTGV
MRQNSQHNIR LVRGSHIVTK RLYDHDKAYF FQGTDGRIIF AIPYEQDFTL IGTTDAEHTD
ADTKPAITDE ERDYLCAFAS EYFEKPVTAE DVVWTYSGVR PLYDDGASSA TAATRDYVLA
LDENGPPVLS VFGGKITTYR KLAEQALAKM GLGEAWTAGV ALPGGDFKVC EVASLTKKLE
ADYPFLDAKW AGRMIRAYGT EAWDVLGDAK TADDLGPDFG ATLTGAELKW MMAREYAVAG
DDALWRRTKL GLRLSAEERA AVDTWMKEHA A
//
