ID A0A1A8XJB6_9RHOO Unreviewed; 538 AA.
AC A0A1A8XJB6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:SBT04033.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:SBT04033.1};
GN ORFNames=PROAA_1190021 {ECO:0000313|EMBL:SBT04033.1};
OS Candidatus Propionivibrio aalborgensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=1860101 {ECO:0000313|EMBL:SBT04033.1, ECO:0000313|Proteomes:UP000199600};
RN [1] {ECO:0000313|EMBL:SBT04033.1, ECO:0000313|Proteomes:UP000199600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2 {ECO:0000313|EMBL:SBT04033.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; FLQY01000023; SBT04033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8XJB6; -.
DR Proteomes; UP000199600; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
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: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 ECO:0000313|EMBL:SBT04033.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199600}.
FT DOMAIN 17..336
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 436..514
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 538 AA; 61382 MW; 07EA928806F20E36 CRC64;
MKLRNSNIQK LDKSVYDVLI IGGGINGAVA AAALSGKGAK VALIEQRDFA GFTSQQSSNL
AWGGIKYLEN HDYGLVRKLC LSRNHLIENY PSRVKEIRFY STVEKGCRFH PLFLWLGTWV
YWFFGSGFTQ IPRWLSRDTV NAEEPVIATG NFYGGFEYSD AYLHDNDSRF VFQFVRTAMD
RGCIAANYLE SLGASRVQDC WLTQARDVLS GEILEIRSKV LINAAGPFVD VHNRLTGERT
EHRHVFSKGI HLIVPRITLN PRILTFFADD GRLFFVIPMG VRTCIGTTDT RVDSPFVEVT
EEDRNFVLGN INKRLNLVQP LTKADIISER CGVRPLVAKS EMSDESGGDW LQLSRKHEID
IDAKQAHISV FGGKLTDCVN VGDEISEIVS GMGINLPHPE YKWYGEPHPS VREEYIHQAR
LMNLDSYTSP EAIESLSSRL WRRYDQQAFE LLAEIREDPR QAEILIKGTD YIRCEIRLAK
HQEMIIKLED FLRRRSKIAL VVKHADIQQA EGLMEACEIL FGDQAREKYD EYFQERSE
//
