ID U1MPM3_9MICO Unreviewed; 608 AA.
AC U1MPM3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=L332_05140 {ECO:0000313|EMBL:ERG63856.1};
OS Agrococcus pavilionensis RW1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agrococcus.
OX NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG63856.1, ECO:0000313|Proteomes:UP000016462};
RN [1] {ECO:0000313|EMBL:ERG63856.1, ECO:0000313|Proteomes:UP000016462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RW1 {ECO:0000313|EMBL:ERG63856.1,
RC ECO:0000313|Proteomes:UP000016462};
RX PubMed=23814108;
RA White R.A.III., Grassa C.J., Suttle C.A.;
RT "First draft genome sequence from a member of the genus agrococcus,
RT isolated from modern microbialites.";
RL Genome Announc. 1:e00391-13(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}.
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:ERG63856.1}.
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DR EMBL; ASHR01000028; ERG63856.1; -; Genomic_DNA.
DR AlphaFoldDB; U1MPM3; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000016462; 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: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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000016462}.
FT DOMAIN 32..392
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 414..538
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 557..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 66083 MW; 557BAF1AA306847E CRC64;
MSETTNSVSR SRKLGPEERA AAIASMRERE VDVLVIGGGI VGTGAALDAV TRGLRVGLIE
ARDFASGTSS RSSKLIHGGI RYLEQLNFGL VREALIERGL LLQRIAPHLA KPVRFLYPLE
TPLIERAYIG AGMALYDVFS YTGFMKPGVP LHRHLTKKQV LKKIPSLDPN AFVGGLTYYD
AQVDDARYVA ELARTASFYG AHVASRVRAE GFLKVGERVV GVQAHDYETG EQFEIRAKQV
VNATGVWTGE TQAMVGERGE FKVRASKGVH LVVPRDRFHS EMGLLLRTAK SVLFVIPWGR
HWIIGTTDTD WNLDKAHPAA TAADIDYILD NVNKVLATKL TRADVEGVYA GLRPLLAAGG
DGTSTANISR EHHVSHTVPG LVLIAGGKWT TYRVMAKDAI DEAVSAMDGK VPESCTDQIP
LLGATGYRAA WNKRAKIARA FGVHKHRVEH LLNRYGVLTD EILDMIRKDP SLLEPLPGAD
DYIGAEVRYA CTHEGALHLD DVLARRTRIS IESWDRGVAA APVAARIMAD ALGWDDARVE
KEINTYNKRV AAEIASQELP DDESADRART EAPEIVPLSA LPTADTVGTR PQEASPAGRG
AGAPPVVE
//
