ID A0A0Q3WQK5_BRECH Unreviewed; 555 AA.
AC A0A0Q3WQK5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=AN963_09095 {ECO:0000313|EMBL:KQL49837.1};
OS Brevibacillus choshinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL49837.1, ECO:0000313|Proteomes:UP000051063};
RN [1] {ECO:0000313|EMBL:KQL49837.1, ECO:0000313|Proteomes:UP000051063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL49837.1,
RC ECO:0000313|Proteomes:UP000051063};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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}.
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:KQL49837.1}.
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DR EMBL; LJJB01000007; KQL49837.1; -; Genomic_DNA.
DR RefSeq; WP_055744160.1; NZ_LJJB01000007.1.
DR AlphaFoldDB; A0A0Q3WQK5; -.
DR STRING; 54911.AN963_09095; -.
DR PATRIC; fig|54911.3.peg.6019; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000051063; 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.
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}.
FT DOMAIN 25..377
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 407..533
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 555 AA; 62196 MW; ABDCAC1F5789A3D1 CRC64;
MHIDTTLSAL QRTTFLNQLT TDRLDLLIIG GGVTGAGIAL DAASRGLTVG LIEKQDFAAG
TSSRSTKLVH GGLRYLKQGD VKLVREVGRE RTILYRNAPH IVVPEKMILP IVEKGTYGKM
ATSIGLYVYD LLAGVKRKER RTMLSKKQTT VAEPLLRTDI LKGSGMYYEY RTDDARLTIE
VIKTARTFGA SCVNYTEATD FIYENGKVIG VKGKDLITGK ELVILAKKIV NAAGPWVDRL
REKDQSLFDK RLHLTKGVHL VVPHARLPLK QAVYFDVADK RMIFAIPRNK STYIGTTDTD
YQGELESPRV TQQDVAYLLR ATNDMFPSVK LTEQDITSSW AGLRPLIHED GKSPSELSRK
DEVFHSASGL ITIAGGKLTG FRKMAERVVD IVTKELIKEE GRAFKSCHTH QIVLAGGSFP
SAAAIPDFIR VQAKRVRSFG IPEASIAELV GKYGRNTDKI VKLALELQKQ RHPAEDAMAL
AELQYGIREE MVMTLRDFLI RRSGKLFFDR KSIGRVYLKI ADEMARTLKW SAIEKEREIK
AFEEEYQQVK SFQLE
//
