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GLPO_LACLA
ID   GLPO_LACLA              Reviewed;         609 AA.
AC   Q9CG65; O07381;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Alpha-glycerophosphate oxidase;
DE            EC=1.1.3.21;
DE   AltName: Full=Glycerol-3-phosphate oxidase;
GN   Name=glpO; Synonyms=glpD; OrderedLocusNames=LL1245; ORFNames=L0013;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-253.
RC   STRAIN=210;
RX   PubMed=9212417; DOI=10.1128/aem.63.7.2702-2707.1997;
RA   Erlandson K., Batt C.A.;
RT   "Strain-specific differentiation of lactococci in mixed starter culture
RT   populations using randomly amplified polymorphic DNA-derived probes.";
RL   Appl. Environ. Microbiol. 63:2702-2707(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate +
CC         H2O2; Xref=Rhea:RHEA:18369, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642; EC=1.1.3.21;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- CAUTION: As L.lactis is unable to produce acid from glycerol, the
CC       significance and/or function of the glpO gene in this organism is at
CC       present unknown. {ECO:0000305}.
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DR   EMBL; AE005176; AAK05343.1; -; Genomic_DNA.
DR   EMBL; AF001829; AAB63270.1; -; Genomic_DNA.
DR   PIR; E86780; E86780.
DR   RefSeq; NP_267401.1; NC_002662.1.
DR   RefSeq; WP_010905845.1; NC_002662.1.
DR   AlphaFoldDB; Q9CG65; -.
DR   SMR; Q9CG65; -.
DR   STRING; 272623.L0013; -.
DR   PaxDb; Q9CG65; -.
DR   EnsemblBacteria; AAK05343; AAK05343; L0013.
DR   KEGG; lla:L0013; -.
DR   PATRIC; fig|272623.7.peg.1346; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   OMA; CIVNAAG; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR   GO; GO:0004369; F:glycerol-3-phosphate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..609
FT                   /note="Alpha-glycerophosphate oxidase"
FT                   /id="PRO_0000126109"
FT   BINDING         21..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        152
FT                   /note="R -> H (in Ref. 2; AAB63270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="K -> R (in Ref. 2; AAB63270)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   609 AA;  67310 MW;  E7A31EA7A2A89236 CRC64;
     MAFSKKTRQE AITKIQNEEM DLLVIGGGIT GAGLTLQAAA AGMKVAVLEM QDFSEGTSSR
     STKLVHGGIR YLKNFDVEVV SDTVSERAVV QGIAPHIPKP DPMLLPIYDD EGKTTFDMFS
     VKIAMDLYDR LAGVDEDSPY ANYTISPEEV LRREPLIKKK GLQGAGVYLD YRNNDARLVI
     DNIKKAVEDG AQAISKMKVI DFIYTDGQIS GIRARDLLTD QVIEVKAKLV INTSGPWVDK
     IRYLNFTRPI VPKMRPTKGV HLVVDAAKLP VPQPTYFDTG KHDKRMVFAI PRENKTYFGT
     TDTDYHGDFT DPKVTQEDVD YLLDVINFRY PEANITINDI EASWAGLRPL LGGNSGSDYN
     GGDNGAVSET SFNAVVEAVL RYKNKTATKA EVEHLLNNME SSLSEKGDAP SSVSRGSSLE
     RESDGLITLA GGKITDYRKM AAGAMELICQ LLEEDFGLKY EPIDSKKYQI SGGEFDPTKV
     EEVVAENMKV GVAAGLTEEE AKYIADFYGM NALQVFAYAS EMEAYEGLSL AESARLCYAL
     EDEMILTPVD YLLRRTNHIL FMREGVDAIK VHVVNAMADD LGWSAEEKAE QEKALEEALR
     ESDLSDLKK
 
 
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