ID A0A0E0TCX7_GEOS2 Unreviewed; 557 AA.
AC A0A0E0TCX7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN OrderedLocusNames=GYMC52_2133 {ECO:0000313|EMBL:ADU94535.1};
OS Geobacillus sp. (strain Y412MC52).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=550542 {ECO:0000313|EMBL:ADU94535.1, ECO:0000313|Proteomes:UP000002223};
RN [1] {ECO:0000313|EMBL:ADU94535.1, ECO:0000313|Proteomes:UP000002223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC52 {ECO:0000313|EMBL:ADU94535.1,
RC ECO:0000313|Proteomes:UP000002223};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mead D., Woyke T.;
RT "Complete sequence of chromosome of Geobacillus sp. Y412MC52.";
RL Submitted (JAN-2011) 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; CP002442; ADU94535.1; -; Genomic_DNA.
DR RefSeq; WP_013524103.1; NC_014915.1.
DR AlphaFoldDB; A0A0E0TCX7; -.
DR KEGG; gya:GYMC52_2133; -.
DR HOGENOM; CLU_015740_5_2_9; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000002223; 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: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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 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}.
FT DOMAIN 21..347
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..529
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 557 AA; 62337 MW; CE6ED973A6D10DB7 CRC64;
MAFSSKHRSD VLQAMSEKQY DLLIIGGGIT GSGIALDAIS RGMTVALVEM QDFAAGTSSR
STKLVHGGLR YLKQFEVKLV AEVGRERAIV YENGPHVTTP EWMLLPIYRG GTFGKWSTSI
GLWLYDRLAG VKQSERRTML NARQTLEKEP LLKRDGLIGG GYYVEYRTDD ARLTIEVIKK
AVELGADAVN YVKAEQFLYD ERGRAIGARC RDMLGGLLYD IRAKKVVNAA GPWVDALRDK
DGSKTGKRLR LTKGVHIVID QKRFPLKQAV YFDTPDGRMV FAIPRDGKTY VGTTDTFYDD
DPAHPAMTEE DRDYLLQAIH YMFPSVGVTA DDVESSWAGV RPLIYEEGKD PSEISRKDEI
WTSPSGLITI AGGKLTGYRK MAETVVDLVA KQLEKEEGKA FGPCRTKQLP ISGGDVGGSH
RLPAFIAEKA EEAVRYGLTK EAGARLARQY GTNVDRLFAL SQQYDRSSGL TRETFIRLVY
AIEEEMAAKP VDYFIRRTGA LLFDIDSVRR EKEEVMAFMA RYLGWTGEER DVYEKELDKE
LRRAVLGRSG VNDPLKE
//