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Q81U58 (GLPK_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycerol kinase
EC=2.7.1.30
Alternative name(s):
ATP:glycerol 3-phosphotransferase
Glycerokinase
Short name=GK
Gene names
Name:glpK
Ordered Locus Names:BA_1026, GBAA_1026, BAS0960
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism. HAMAP MF_00186

Catalytic activity

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

Pathway

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

Sequence similarities

Belongs to the FGGY kinase family.

Ontologies

Keywords
   Biological processGlycerol metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycerol-3-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycerol kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Glycerol kinase HAMAP MF_00186
PRO_0000059431

Regions

Nucleotide binding410 – 4145ATP By similarity

Sites

Binding site121Substrate By similarity
Binding site161ATP By similarity
Binding site821Substrate By similarity
Binding site1341Substrate By similarity
Binding site2441Substrate By similarity
Binding site2661ATP By similarity
Binding site3091ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81U58 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5CB03262F9AFC931

FASTA49655,057
        10         20         30         40         50         60 
MKKYILSLDQ GTTSSRAILF NKKGEIVHSA QKEFTQHFPK PGWVEHNAQE IWGSILAVIA 

        70         80         90        100        110        120 
TCLSEADVKP EQIAGIGITN QRETAVVWDK TTGKPIYNAI VWQSRQTAEI CDELKEKGYS 

       130        140        150        160        170        180 
EMVREKTGLL IDAYFSGTKV KWILDNVEGA REKAENGDLL FGTIDTWLVW KLSGGKAHVT 

       190        200        210        220        230        240 
DYSNASRTLM FNIHDLQWDD ELLDMLTVPK SMLPEVRPSS EVYGETIDYH FFGQNVPIAG 

       250        260        270        280        290        300 
VAGDQQAALF GQACFGEGMA KNTYGTGCFM LMNTGEKAVA SEHGLLTTIA WGIDGKVNYA 

       310        320        330        340        350        360 
LEGSIFVAGS AIQWLRDGMR MFKDASESEV YASRVESTDG VYVVPAFVGL GTPYWDSEVR 

       370        380        390        400        410        420 
GAMFGVTRGT TKEHFIRATL ESLAYQIKDV LCAMEADSGI ELKTLRVDGG AVKNNFLMKF 

       430        440        450        460        470        480 
QSDILDVPVE RPVINETTAL GAAYLAGLAV GYWKNQDEIK EQWHMDKRFE PTMEAETSEE 

       490 
LYAGWKKAIE ATKAFK

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016879 Genomic DNA. Translation: AAP25013.1.
AE017334 Genomic DNA. Translation: AAT30129.1.
AE017225 Genomic DNA. Translation: AAT53285.1.
RefSeqNP_843527.1. NC_003997.3.
YP_017654.1. NC_007530.2.
YP_027234.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81U58.
SMRQ81U58. Positions 4-489.
ModBaseSearch...

Protein-protein interaction databases

IntActQ81U58. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000012447; EBBACP00000012203; EBBACG00000012439.
EBBACT00000016971; EBBACP00000016592; EBBACG00000016962.
EBBACT00000023168; EBBACP00000022653; EBBACG00000023159.
GeneID1088947.
2814984.
2850883.
GenomeReviewsGene locus BA_1026 in contig AE016879_GR.
Gene locus BAS0960 in contig AE017225_GR.
Gene locus GBAA_1026 in contig AE017334_GR.
KEGGban:BA_1026.
bar:GBAA_1026.
bat:BAS0960.
TIGRBA_1026.
GBAA_1026.

Phylogenomic databases

GeneTreeEBGT00050000001374.
HOGENOMHBG511469.
OMAALYGQLC.
ProtClustDBPRK00047.

Enzyme and pathway databases

BioCycBANT260799:BAS0960-MONOMER.
BANT261594:GBAA1026-MONOMER.

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 nameGLPK_BACAN
AccessionPrimary (citable) accession number: Q81U58
Secondary accession number(s): Q6I2E6, Q6KW74
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents