ID A0A1S2MDP1_9BACI Unreviewed; 560 AA.
AC A0A1S2MDP1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-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=AWH56_002215 {ECO:0000313|EMBL:QOY36516.1}, AWH56_04110
GN {ECO:0000313|EMBL:OIJ22858.1};
OS Anaerobacillus isosaccharinicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=1532552 {ECO:0000313|EMBL:OIJ22858.1, ECO:0000313|Proteomes:UP000180175};
RN [1] {ECO:0000313|EMBL:OIJ22858.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:OIJ22858.1,
RC ECO:0000313|Proteomes:UP000180175};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOY36516.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY36516.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=28104661;
RA Bassil N.M., Lloyd J.R.;
RT "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT Anaerobacillus Genus.";
RL Genome Announc. 5:e01493-16(2017).
RN [3] {ECO:0000313|EMBL:QOY36516.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY36516.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=29580368;
RA Bassil N.M., Lloyd J.R.;
RT "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT degrades isosaccharinic acid.";
RL Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
RN [4] {ECO:0000313|EMBL:QOY36516.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY36516.1};
RA Bassil N.M., Lloyd J.R.;
RL Submitted (OCT-2020) 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|ARBA:ARBA00000153,
CC 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 -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
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; LQXD01000019; OIJ22858.1; -; Genomic_DNA.
DR EMBL; CP063356; QOY36516.1; -; Genomic_DNA.
DR RefSeq; WP_071315919.1; NZ_CP063356.1.
DR AlphaFoldDB; A0A1S2MDP1; -.
DR KEGG; aia:AWH56_002215; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000180175; Chromosome.
DR Proteomes; UP000180175; 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:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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 Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000180175}.
FT DOMAIN 23..378
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 401..529
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 560 AA; 62871 MW; 9719B82BAF10C46B CRC64;
MGNPFSSIQR VNYLKEMSNQ ELDLLVIGGG ITGAGIALDA QVRGIKTGLI EMQDFGAGTS
SRSTKLVHGG LRYLKQFEVK LVAEVGKERA IVYENAPHVT TPEWMLLPMI EGGTFGKLAT
SFGLKVYDFL AGVRKSERRF MLNKQQTMEK EPLLRKDKLK GGGVYVEYKT DDARLTLEIM
KEAVARGVLA VNYAKADGFI YENKKIVGVK VVDQFSGEVT EIRAKKIVNA AGPWVDTLRE
KDNSKKGKYL HLTKGVHLVF DESRFPLKQA VYFDTEKDGR MCFAIPRDGK TYVGTTDTYY
KSDITHPRMT VADREYIIDA VNYMFPEVKL KAKDVESCWT GLRPLIHEEG KSASEISRKD
EIFFSDSGLI SIAGGKLTGY RKMAERIVGI VGKDLGINKP CTTEIIKLSG GDIGGSVNLP
KFLEEKTKEG MQLGLTKKEA LKLTKLYGTN VNKVYDIIRT KGADAKRYGL TEEVFGALVY
GIEEEMVATP VDFFNRRTGA IFFNIDWVRS WKEPVLQYMK QRFNWTAEEV NSHKLRVDQE
IEHATVPVDE VVEVERKNAI
//
