ID A0A0Q7B934_9ACTN Unreviewed; 578 AA.
AC A0A0Q7B934;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=ASC77_10855 {ECO:0000313|EMBL:KQW49183.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW49183.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW49183.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW49183.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW49183.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW49183.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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|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:KQW49183.1}.
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DR EMBL; LMDV01000008; KQW49183.1; -; Genomic_DNA.
DR RefSeq; WP_056153200.1; NZ_LMDV01000008.1.
DR AlphaFoldDB; A0A0Q7B934; -.
DR STRING; 1736439.ASC77_10855; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000051939; 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; 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.
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:UP000051939}.
FT DOMAIN 29..390
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 416..540
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 578 AA; 62866 MW; 6C6DB2086E4B565E CRC64;
MTRSSALGPD ARDQALAAMS GVAGQGELDV LVVGGGIVGV GTALDAVTRG LSTGLVEQRD
IASGTSSRSS KLIHGGLRYL EMLDFGLVRE ALQERGLLLT RLAPHLVRPV PFLYPLTHRG
WERPYVGAGL ALYDGMAMLG KAEMGVPRHR HLFRRQVARI APDFKTETIS GAIRYYDCQV
DDARLALTIA RTAAAHGAHV ATRVQVVGFL REGERVVGVR ARDLEAGPDS PEIEIRARVV
VNAAGVWTDE IQEMVGGRGS LHVQASKGIH LVVPRDRIRS EAGFIVRTEK SVLFVIPWGR
HWIIGTTDTP WSLDKAHPAA SKADIDYILN HVNAILREPL DHEDVEGVYA GLRPLLSGES
EPTSRISREH TVVTPVPGLV MIAGGKLTTY RVMGRDAVDA AAHSLRTTVN LTIRDSITDR
VPLLGAADWE TRSNQRVLLA RRSGLHVARI DHLLGRYGGL VDEVLELVSS RRSLGAPLEG
AEDYLAAEVV YAVTHEGARH LDDLLTRRTR ISIETFDRGV GAAPGVAALM AGELGWDAAR
TADEVDHYRR RVEAERQSQL KLTDQEADEA RVKVADIV
//
