ID A0A2N0Z1K7_9BACI Unreviewed; 557 AA.
AC A0A2N0Z1K7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=CWS01_12325 {ECO:0000313|EMBL:PKG23394.1};
OS Niallia nealsonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=115979 {ECO:0000313|EMBL:PKG23394.1, ECO:0000313|Proteomes:UP000233375};
RN [1] {ECO:0000313|EMBL:PKG23394.1, ECO:0000313|Proteomes:UP000233375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-92 {ECO:0000313|EMBL:PKG23394.1,
RC ECO:0000313|Proteomes:UP000233375};
RX PubMed=12656168; DOI=10.1099/ijs.0.02311-0;
RA Venkateswaran K., Kempf M., Chen F., Satomi M., Nicholson W., Kern R.;
RT "Bacillus nealsonii sp. nov., isolated from a spacecraft-assembly facility,
RT whose spores are gamma-radiation resistant.";
RL Int. J. Syst. Evol. Microbiol. 53:165-172(2003).
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:PKG23394.1}.
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DR EMBL; PISE01000025; PKG23394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0Z1K7; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000233375; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233375}.
FT DOMAIN 20..349
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 401..530
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 557 AA; 62583 MW; B1EC2E8D01BE46B6 CRC64;
MQMTNRQEIE QQLKTHKYEV LIIGGGITGA GIALDAATRG MKTALVEMQD FSAGTSSRST
KLVHGGLRYL KQLEVGMVAE VGKERAVVYE NGPHVTTPEW MLLPFHKGGT FGKFTTSIGL
RVYDFLAGVK KAERRTMFSK EETLLKEPLI KKENLKGGGY YVEYRTDDSR LTIEVMKKAI
EKGADALNYT KVEKLLYDKK GKINGAFVKN MLTGEKYSIF AEYVVNAAGP WVDTIREIDG
SKKGKALQLT KGVHIVIDQR KFPLKQAIYF DTPDKRMVFA IPREGKAYVG TTDTFYGDDP
VSPTMQVEDR DYLINAIHYM FPSVKISTAD IESSWAGVRP LILEDGKDPS EISRKDEIWE
SESGLITIAG GKLTGYRKMA QTVTDLVAKH FEKNGKTFRS CLTKHLPISG GDVGGATHFK
EFQLKHLEKG VDAGLTESDA LAIVNKYGSN AESIYQLVKE NKQEAVLYSL PMLLWAKIRY
AMEGEMAVTP VDVLLRRTGL ILFHIQEVQT YKSQVVQYME EYLNWSKEER DKFTKELEKE
ILNATVPEDE ENKAKLA
//
