ID A1K961_AZOSB Unreviewed; 529 AA.
AC A1K961;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:CAL95366.1};
DE EC=1.1.99.5 {ECO:0000313|EMBL:CAL95366.1};
GN Name=glpA {ECO:0000313|EMBL:CAL95366.1};
GN OrderedLocusNames=azo2750 {ECO:0000313|EMBL:CAL95366.1};
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL95366.1, ECO:0000313|Proteomes:UP000002588};
RN [1] {ECO:0000313|EMBL:CAL95366.1, ECO:0000313|Proteomes:UP000002588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72 {ECO:0000313|EMBL:CAL95366.1,
RC ECO:0000313|Proteomes:UP000002588};
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL95366.1; -; Genomic_DNA.
DR RefSeq; WP_011766476.1; NC_008702.1.
DR AlphaFoldDB; A1K961; -.
DR STRING; 62928.azo2750; -.
DR KEGG; azo:azo2750; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_4_1_4; -.
DR Proteomes; UP000002588; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; PS00978; FAD_G3PDH_2; 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:CAL95366.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002588}.
FT DOMAIN 23..379
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 419..498
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 529 AA; 55693 MW; 8FBFC67EE0067A97 CRC64;
MSGPPGQSRA ALLARLRADP VWDVLVVGGG ASGLGCAVDA AARGYQVALV EARDFAQGTS
SRSTKLIHGG VRYLAQGRLG LVREALHERA RLLENAPHLV RPLRFVVPAR RWSELATVGA
GLGLYDLLAG RGGIGRSRLL GAAETRAALP GVKADGLCGG VAYWDAQFDD ARLALALART
LADLGGVPLN HCALERLLIE DGVIRGAVVR DTERAEPFAL RARVVINATG VWSDQVRRLA
NPAAPATLRP SQGVHLVVDR AFLPGRQALL VPRTEDGRVL FMIPWQDRLL LGTTDTARAD
LPLEPEALPG EVDFILSTAA RYLERAPGRA DVLSVFAGLR PLLESAAARN SGELSREHVV
EVSAQGLVSM LGGKWTTYRS MAADAVDAAI EWAGLPARPC ATASLRLHGA AAPRGDRLDA
YGSDLSGLES LPGAGRVLVE GLDLTEAEVR HAARAEWARG VEDVLARRHR ALFLDATLAA
CAAPAVAQIL AAELGRDEGW VAAQTDAFHA LASAYGASLS RACAAARSG
//
