ID M9YBZ7_AZOVI Unreviewed; 510 AA.
AC M9YBZ7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:AGK18014.1};
GN ORFNames=AvCA6_45730 {ECO:0000313|EMBL:AGK18014.1};
OS Azotobacter vinelandii CA6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1283331 {ECO:0000313|EMBL:AGK18014.1, ECO:0000313|Proteomes:UP000012988};
RN [1] {ECO:0000313|EMBL:AGK18014.1, ECO:0000313|Proteomes:UP000012988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CA6 {ECO:0000313|EMBL:AGK18014.1,
RC ECO:0000313|Proteomes:UP000012988};
RX PubMed=23792740; DOI=10.1128/genomeA.00313-13;
RA Noar J.D., Bruno-Barcena J.M.;
RT "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain CA
RT and Tungsten-Tolerant Mutant Strain CA6.";
RL Genome Announc. 1:E00313-E00313(2013).
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}.
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DR EMBL; CP005095; AGK18014.1; -; Genomic_DNA.
DR RefSeq; WP_012703052.1; NC_021150.1.
DR AlphaFoldDB; M9YBZ7; -.
DR KEGG; avd:AvCA6_45730; -.
DR PATRIC; fig|1283331.3.peg.4376; -.
DR HOGENOM; CLU_015740_5_0_6; -.
DR Proteomes; UP000012988; Chromosome.
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; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 13..365
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 388..497
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 510 AA; 57553 MW; 3058D266E32A05C2 CRC64;
MSPSNSSNAE LYDIAVIGGG INGAGIAADA AGRGLSVFLC EQDDLARHTS SASSKLIHGG
LRYLEHYEFR LVREALAERE VLLAKAPHIV KPLRFVLPHR PHLRPAWMIR AGLFLYDHLG
KRKKLPGSRG LRFGARSPLK AEIRRGFEYS DCWVDDARLV VLNAMAAREH GAQVHTRTRC
LSASRQRDHW HLQLERADGS AFSIRAKALV NAAGPWVARF IETGLQQKAP YGIRLIQGSH
LIVPRLYEGE HAYILQNEDR RIVFAIPYLE RFTLIGTTDR EYRDDPAQVR ISEEETDYLL
AVVNRHFKYQ LSRDSILHSY SGVRPLCNDE SADPSAVTRD YTLALSGIPG EPPLLSVFGG
KLTTYRKLAE AALEQLAPFF PQMKARWTAE KPLPGGEQMS DSRTLADQLR QRHAWLAPEL
ARRWATTYGS RAWRLLENVN GPADLGEHFG ATLHAHEVDY LCAQEWAREA EDILWRRSKL
GLFLSLEEQE RLRAYLDATT RHLEAHVLAS
//
