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Q4L608 (GLPD_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aerobic glycerol-3-phosphate dehydrogenase

EC=1.1.5.3
Gene names
Name:glpD
Ordered Locus Names:SH1608
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.

Cofactor

FAD By similarity.

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic route): step 1/1.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycerol metabolism
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycerol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

glycerol-3-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentglycerol-3-phosphate dehydrogenase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionsn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Aerobic glycerol-3-phosphate dehydrogenase
PRO_0000270067

Regions

Nucleotide binding21 – 4929FAD Potential

Sequences

Sequence LengthMass (Da)Tools
Q4L608 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 0856390DC2F7AB13

FASTA55762,821
        10         20         30         40         50         60 
MALSTLNREV IKKNLQNEEY DVVIIGGGIT GAGIALDASQ RGMKVALVEM QDFAQGTSSR 

        70         80         90        100        110        120 
STKLVHGGLR YLKQAQIKVV AETGKERAIV YENGPHVTTP EWMLLPMHKG GTFGKFTTNL 

       130        140        150        160        170        180 
GLTAYDRLAG VKKYERKKML SKKQTLNKEP LVKKDGLKGG GYYVEYRTDD ARLTIEVMKR 

       190        200        210        220        230        240 
AEENGAEILN HTKSTDFIYD SKSKVRGIEV QDLLTGEMYE INAKKVINAA GPWVDEVRKK 

       250        260        270        280        290        300 
DYTRNNKQLR LTKGVHVVID QSKFPLRQAV YFDTEKDGRM IFAIPREGKA YVGTTDTFYD 

       310        320        330        340        350        360 
NDKTKPLTTQ EDRDYLIDAI NYMFPDVNVK DEDIESTWAG VRPLILEDGK DPSEISRKDE 

       370        380        390        400        410        420 
IWEGKSGLLT IAGGKLTGYR HMALEIVDLL AKRLKQEYKL TFAECKTKHT PISGGDVGGS 

       430        440        450        460        470        480 
ANFESFVERK VEEGKAIGLQ ADVAKRLASK YGSNVDKLYN IAQIAQDKDL KLPLELYVEL 

       490        500        510        520        530        540 
VYSVQNEMVF KPTDFLIRRS GKLYFNINEV KQYKDAVVEE LAKLLNYTQS QQNEFTKEIN 

       550 
IAIEEATRGN EQLAVLK 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE04917.1.
RefSeqYP_253523.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH1608.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE04917; BAE04917; SH1608.
GeneID3482224.
KEGGsha:SH1608.
PATRIC19619321. VBIStaHae67511_1584.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0578.
HOGENOMHOG000004812.
KOK00111.
OMAYAKVDSF.
OrthoDBEOG651SR7.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-1662-MONOMER.
UniPathwayUPA00618; UER00674.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
PRINTSPR01001. FADG3PDH.
PROSITEPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLPD_STAHJ
AccessionPrimary (citable) accession number: Q4L608
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: August 2, 2005
Last modified: May 14, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways