ID K2GFM1_9BACI Unreviewed; 554 AA.
AC K2GFM1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=MJ3_00615 {ECO:0000313|EMBL:EKE32957.1};
OS Salimicrobium jeotgali.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE32957.1, ECO:0000313|Proteomes:UP000011746};
RN [1] {ECO:0000313|EMBL:EKE32957.1, ECO:0000313|Proteomes:UP000011746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE32957.1,
RC ECO:0000313|Proteomes:UP000011746};
RX PubMed=23144427; DOI=10.1128/JB.01808-12;
RA Lee S.H., Jung J.Y., Jeon C.O.;
RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT Myulchi-Jeot, Korean Fermented Seafood.";
RL J. Bacteriol. 194:6695-6695(2012).
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:EKE32957.1}.
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DR EMBL; AMPQ01000001; EKE32957.1; -; Genomic_DNA.
DR RefSeq; WP_008587089.1; NZ_LT899438.1.
DR AlphaFoldDB; K2GFM1; -.
DR STRING; 1230341.AAV35_003400; -.
DR KEGG; sje:AAV35_003400; -.
DR PATRIC; fig|1230341.3.peg.135; -.
DR eggNOG; COG0578; Bacteria.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000011746; 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:UP000011746}.
FT DOMAIN 21..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..531
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 554 AA; 62584 MW; F329B00A4B43D945 CRC64;
MSFSSYERKE QFRKLTEEQW DVLVIGGGIT GAGIALDASS RGMNTALVEM QDYAAGTSSR
STKLVHGGLR YLKQFEVKMV AEVGKEREIV YENGPHVTTP EWMMLPFYKE GNFGPYSTNL
GLMVYDFLAG VKKAERRRMF SPEEAMEREP LVNGENLKGA GFYVEYKTDD ARLTLDVMKK
AEEFGATAAN YAKVTDFIYE NGKVTGAVVE DTITGDTYQV KAKKIINAGG PWVDTLREKD
GSKKGKSLRL TKGIHLVFDQ STFPLHQAIY FDSPDGRMIF AIPRDGKAYI GTTDTVYEGD
IAHPTMTVED RDYLLRALKS MFPHVNVTKD DVESSWAGLR PLIYEEGKDP SEISRKDEIF
VSDSGLISMA GGKLTGYRKM AEDAVDLIRD QLAKDYGVYF GDTDTVHIPV SGGEVGGSEG
FEKFQYEKVI EGVKLGLEKE EAERLVSFYG ANVDKLYALY EENKVKAGEE EIDPVVFTQL
IYALKEEQTY KPVDFFIRRT GALFFNINFV REHKDNVIRY MAKELEWTEE QTNEYKEELE
QLLIEAVKPV EYAR
//
