ID A0A1C3JXZ2_9BURK Unreviewed; 518 AA.
AC A0A1C3JXZ2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Aerobic glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:SBT24045.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:SBT24045.1};
GN ORFNames=ODI_03464 {ECO:0000313|EMBL:SBT24045.1}, ODI_R3666
GN {ECO:0000313|EMBL:SOE51761.1};
OS Orrella dioscoreae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Orrella.
OX NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT24045.1, ECO:0000313|Proteomes:UP000078558};
RN [1] {ECO:0000313|EMBL:SBT24045.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT24045.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SOE51761.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE51761.1};
RA de Groot N.N.;
RL Submitted (AUG-2017) 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; FLRC01000005; SBT24045.1; -; Genomic_DNA.
DR EMBL; LT907988; SOE51761.1; -; Genomic_DNA.
DR RefSeq; WP_067749823.1; NZ_LT907988.1.
DR AlphaFoldDB; A0A1C3JXZ2; -.
DR STRING; 1851544.ODI_03464; -.
DR KEGG; odi:ODI_R3666; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000078558; Chromosome i.
DR Proteomes; UP000078558; 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; 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.
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:SBT24045.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078558}.
FT DOMAIN 16..378
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 401..507
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 518 AA; 57115 MW; E6C8B819138FF204 CRC64;
MSDFLPPPPP DHHEVDLLVV GGGINGAGIV RDAAGRGLKV LLCERGDLAQ ATSSSSSKLV
HGGLRYLENR EFRLVREALA EREVLLTNAA HIVHPMRFVL PHDATLRPAW MLRTGLFLYD
HLARRSPRLP GARRLDLRAD PMGQPLRDDL RTGFAYSDCS VDDARLVVLN AMDAQARGAV
ILTRHECVAA QARDGAWQAR LRGPEGQDVS VRARILVNAA GPWVQALQSL ISTQAGAPPG
PSRLKLVKGS HFTVPKLYDG EHAYILQNDD RRIIFVLPYQ GEFSLIGTTD VAFEGDPGQA
KISDEEIAYL CRAVNRYFKQ QIGPADIAWR YAGVRPLYDD HPDDARLSTV TRDYVFDVAG
GQDGQPVLLS IYGGKITTFR QLAQHAMEKL APYTGKPEAW TASAPLPGSD MPGADPQAYL
HALQERYRWL PAPLARRYVY TYGTLTEQLL AGAQSMEDLG EDFGAGLTEA EVRWLTRHEW
ARTAEDILWR RTRLGLLAPA DAADRLDAWL AQASTADA
//