ID A0A368T4F4_9ACTN Unreviewed; 588 AA.
AC A0A368T4F4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=DEF24_13695 {ECO:0000313|EMBL:RCV58351.1};
OS Marinitenerispora sediminis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Marinitenerispora.
OX NCBI_TaxID=1931232 {ECO:0000313|EMBL:RCV58351.1, ECO:0000313|Proteomes:UP000253318};
RN [1] {ECO:0000313|EMBL:RCV58351.1, ECO:0000313|Proteomes:UP000253318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPS81 {ECO:0000313|EMBL:RCV58351.1,
RC ECO:0000313|Proteomes:UP000253318};
RA Ng Z.Y., Tan G.Y.A.;
RT "Novel actinobacteria from marine sediment.";
RL Submitted (APR-2018) 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|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:RCV58351.1}.
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DR EMBL; QEIN01000097; RCV58351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368T4F4; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000253318; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000253318}.
FT DOMAIN 24..381
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..528
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 544..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 64425 MW; 1D4F6D3CFD2995C0 CRC64;
MTAARLGPEE RAAALAHMAG NELDLLVIGG GIVGAGVALD AVSRGLTVGL VEARDFASGT
SSRSSKLIHG GLRYLEQLDF ELVREALTER GLLLQRIAPH LVRPVPFLYP LRGHVWERGY
VGAGVTLYDT LSLSMGSVRG LPHHRHLTRS GAMRVFPALR RDALVGAVQY WDAQVDDARY
VVTVLRTAAT YGARIASRVQ AVGFLREGEH VTGAEVVDLE TGEELSVRAK QVVNATGVWT
DDIQELVGGR GQIHVRASKG IHLVVPRDRI QASSGLILRT EKSVLFVIPW GRHWIIGTTD
TDWDLDKAHP AASRTDIDYI LDHVNQVLRV PLTRDDVEGV YAGLRPLLYG ESDDTSKLSR
EHTVAHPVPG LVLIAGGKYT TYRVMAKDAV DAVAHGLGGG VPESVTDRVP LVGADGYAAL
WNQRRTLARQ SGLHVSRVQH LLRRYGSMIH EVLALIAERP DLREPLTGAD DYLRAEVVYA
ARYESARHLD DVLSRRTRIS IETWDRGIAV AEEAAALMAE PLGWTEEQVK REVEYYRKRI
EAERAAQEQE NDHEADAVQH GAPDIVPEAP RVPAGGTAAD RMAIREEG
//
