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B4U4L7 (B4U4L7_STREM) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate By similarity. HAMAP-Rule MF_00186

Catalytic activity

ATP + glycerol = ADP + sn-glycerol 3-phosphate. HAMAP-Rule MF_00186 SAAS SAAS018483

Enzyme regulation

Activated by phosphorylation and inhibited by fructose 1,6-bisphosphate (FBP) By similarity. HAMAP-Rule MF_00186

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. HAMAP-Rule MF_00186 SAAS SAAS018483

Subunit structure

Homotetramer and homodimer (in equilibrium) By similarity. HAMAP-Rule MF_00186

Post-translational modification

The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylation, which leads to the activation of the enzyme By similarity. HAMAP-Rule MF_00186

Sequence similarities

Belongs to the FGGY kinase family. HAMAP-Rule MF_00186 RuleBase RU003733

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding14 – 163ATP By similarity HAMAP-Rule MF_00186
Nucleotide binding412 – 4165ATP By similarity HAMAP-Rule MF_00186
Region84 – 852Substrate binding By similarity HAMAP-Rule MF_00186
Region246 – 2472Substrate binding By similarity HAMAP-Rule MF_00186

Sites

Binding site141Substrate By similarity HAMAP-Rule MF_00186
Binding site181ATP By similarity HAMAP-Rule MF_00186
Binding site1361Substrate By similarity HAMAP-Rule MF_00186
Binding site2681ATP By similarity HAMAP-Rule MF_00186
Binding site3111ATP; via carbonyl oxygen By similarity HAMAP-Rule MF_00186
Binding site3151ATP; via amide nitrogen By similarity HAMAP-Rule MF_00186
Binding site3301ATP By similarity HAMAP-Rule MF_00186

Amino acid modifications

Modified residue2321Phosphohistidine; by HPr By similarity HAMAP-Rule MF_00186

Sequences

Sequence LengthMass (Da)Tools
B4U4L7 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: D17BBAB057591E0B

FASTA50155,411
        10         20         30         40         50         60 
MGTETYIMAI DQGTTSSRAI IFNKKGEALV SSQKEFPQLF PQAGWVEHNA NHIWNSVQSV 

        70         80         90        100        110        120 
IADAFIESGI KPEQIEAIGI TNQRETTVVW DKQTGLPIYN AIVWQSRQTA SIAEQLKRDG 

       130        140        150        160        170        180 
YTKMIHEKTG LVIDAYFSAT KLRWLLDHVP GAQERAERGE LLFGTIDTWL VWKLTDGAVH 

       190        200        210        220        230        240 
VTDYSNAART MLYNIKELKW DDEILTLLNI PRAMLPEVRS NSEIYGKTAP FHFYGGEVVI 

       250        260        270        280        290        300 
AGMAGDQQAA LFGQLAFEPG MVKNTYGTGS FIIMNTGQEA QLSSSNLLTT IGYGINGKVY 

       310        320        330        340        350        360 
YALEGSIFIA GSAVQWLRDG LRMIKTSFES EQLALASTNA DEVYVVPAFT GLGAPYWDSN 

       370        380        390        400        410        420 
ARGSVFGLTR GTTKEDFVKA TLQSIAYQVR DVIDTMQVDS GITIQQLRVD GGAAMNNMLM 

       430        440        450        460        470        480 
QFQADILGID IARAKNLETT ALGAAFLAGL AVGYWKDMET LKQLNATGQL FKASMSESRR 

       490        500 
EKLYQGWKRA VKATQFFAEE L 

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References

[1]"Genome sequence of a Lancefield group C Streptococcus zooepidemicus strain causing epidemic nephritis: new information about an old disease."
Beres S.B., Sesso R., Pinto S.W., Hoe N.P., Porcella S.F., Deleo F.R., Musser J.M.
PLoS ONE 3:E3026-E3026(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGCS10565 EMBL ACG62934.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001129 Genomic DNA. Translation: ACG62934.1.
RefSeqYP_002123947.1. NC_011134.1.

3D structure databases

ProteinModelPortalB4U4L7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING552526.Sez_1603.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG62934; ACG62934; Sez_1603.
GeneID6761393.
KEGGsez:Sez_1603.
PATRIC19657180. VBIStrEqu17662_1635.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0554.
HOGENOMHOG000222134.
KOK00864.
OMAHFFGVEV.
OrthoDBEOG6RZB46.

Enzyme and pathway databases

BioCycSEQU552526:GH4P-1632-MONOMER.
UniPathwayUPA00618; UER00672.

Family and domain databases

HAMAPMF_00186. Glycerol_kin.
InterProIPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01311. glycerol_kin. 1 hit.
PROSITEPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB4U4L7_STREM
AccessionPrimary (citable) accession number: B4U4L7
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)