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A9I1F8 (A9I1F8_BORPD) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 34. 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 namesRecommended name:
Glycerol kinase HAMAP MF_00186
EC=2.7.1.30 HAMAP MF_00186
Alternative name(s):
ATP:glycerol 3-phosphotransferase HAMAP MF_00186
Glycerokinase HAMAP MF_00186
Gene names
Name:glpK HAMAP MF_00186 EMBL CAP40857.1
Ordered Locus Names:Bpet0525
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism By similarity. HAMAP MF_00186 SAAS SAAS018483

Catalytic activity

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

Pathway

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

Sequence similarities

Belongs to the FGGY kinase family. HAMAP MF_00186 RuleBase RU003733

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding417 – 4215ATP By similarity HAMAP MF_00186

Sites

Binding site131Substrate By similarity HAMAP MF_00186
Binding site171ATP By similarity HAMAP MF_00186
Binding site831Substrate By similarity HAMAP MF_00186
Binding site1351Substrate By similarity HAMAP MF_00186
Binding site2441Substrate By similarity HAMAP MF_00186
Binding site2661ATP By similarity HAMAP MF_00186
Binding site3161ATP; via carbonyl oxygen By similarity HAMAP MF_00186

Sequences

Sequence LengthMass (Da)Tools
A9I1F8 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: D6366C2DC6C466DE

FASTA50654,505
        10         20         30         40         50         60 
MTKSFILALD QGTTSSRAIV FDRQGQARGV GQREFRQYYP QPGWVEHDAG EIWQSQLDVA 

        70         80         90        100        110        120 
REALRNAGAS AADVAAIGIT NQRETTLIWD RASGRPLARA LVWQDRRTAP LCDKLREQGH 

       130        140        150        160        170        180 
DRLLQARTGL VLDAYFSGTK LAWLLDNVPG ARQAAQRGEL AFGTVDTWLV WQLTGGQVHS 

       190        200        210        220        230        240 
TDPSNASRTL LYDIHTQDWN DEILALLDIP RSVLPSVAPS SAEVGRALPE WFGGPIPIAG 

       250        260        270        280        290        300 
IAGDQQAATF GQACFKPGMA KNTYGTGCFM LMNVGDAPVA SRNNLLSTIG WGLPGQGAGP 

       310        320        330        340        350        360 
AGRPTYMLEG GVFMAGAAVQ WLRDGLGIIQ RSDQVEALAA SVPDTDDVFL VPAFAGLGAP 

       370        380        390        400        410        420 
DWDPYARGTL VGLTRGTTRA HVARATLEAI ALQSAELLTC MNADSGIGLS ELRVDGGAAR 

       430        440        450        460        470        480 
NDLLMQMQTD LLGVPVVRPR VSESTARGAA GLAGLAVGFW SGMEEFAGQW EAERRFEPRW 

       490        500 
NADQRAARLA RWRQAVEHAK GWARPA

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM902716 Genomic DNA. Translation: CAP40857.1.
RefSeqYP_001629128.1. NC_010170.1.

3D structure databases

ProteinModelPortalA9I1F8.
SMRA9I1F8. Positions 5-504.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9I1F8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5818492.
GenomeReviewsGene locus Bpet0525 in contig AM902716_GR.
KEGGbpt:Bpet0525.
PATRIC21162501. VBIBorPet31633_0530.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG511469.
OMASIAYQSN.
ProtClustDBPRK00047.

Family and domain databases

HAMAPMF_00186. Glycerol_kin.
[Tree]
InterProIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
KOK00864.
PANTHERPTHR10196. FGGY_kin. 1 hit.
PTHR10196:SF9. Glycerol_kin. 1 hit.
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 nameA9I1F8_BORPD
AccessionPrimary (citable) accession number: A9I1F8
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info