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Reviewed, UniProtKB/Swiss-Prot Q5P212 (GLPK_AZOSE)

Last modified November 3, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: AZOSEA25270
ORF Names: ebA4462
OrganismAzoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

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Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism By similarity.

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.

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Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glycerol kinase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Glycerol kinase HAMAP MF_00186
PRO_1000098714

Regions

Nucleotide binding408 – 4125ATP By similarity

Sites

Binding site111Substrate By similarity
Binding site151ATP By similarity
Binding site811Substrate By similarity
Binding site1331Substrate By similarity
Binding site2421Substrate By similarity
Binding site2641ATP By similarity
Binding site3071ATP; via carbonyl oxygen By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5P212-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 025DF36EF33D59C9

FASTA49652,577
        10         20         30         40         50         60 
MSYLLALDQG TTSSRALVLD RDGQVKGAAQ QTFAQHYPQP GWVEHDPAEI LATQFDCART 

        70         80         90        100        110        120 
ALERAGVAAS ALAAVGITNQ RETTLLWERS TGRALAPAIV WQDRRTAAAC DRLREAGHAD 

       130        140        150        160        170        180 
TIRASTGLEV DAYFSATKLA WLLDHVPGAR ARARAGELAF GTVDSWLVWH LSGGALHVTD 

       190        200        210        220        230        240 
AGNASRTMLF NIHRCEWDET LLALLDIPPA LLPRVVDSSG VCGTTCAEVL GAAVPIAGIG 

       250        260        270        280        290        300 
GDQQAATFGQ ACFAPGMAKN TYGTGCFLLM NTGAAPVTST NRLLTTIGWR SRGETCYALE 

       310        320        330        340        350        360 
GSIFIGGALV QWLRDGLGLI RRAEDVEALA ASVPDSEGVV LVPAFTGLGA PYWDAYARGT 

       370        380        390        400        410        420 
LFGLTRGTGA AHIARAALEA IALQTVDLVA AMDRDGAGPL AELRVDGGAA ANDLLMQIQA 

       430        440        450        460        470        480 
DLLGVPVVRP KMLETTALGA AYLAGLGVGM WSGIEELASH WRAERRFEPV MAEDRREAAI 

       490 
ARWRRAVERA RGWVAA

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References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CR555306 Genomic DNA. Translation: CAI08652.1.
RefSeqYP_159553.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P212.

Genome annotation databases

GeneID3179823.
GenomeReviewsGene locus AZOSEA25270 in contig CR555306_GR.
KEGGeba:ebA4462.
NMPDRfig|76114.4.peg.2823.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5P212.
OMAIAQREFT.

Enzyme and pathway databases

BioCycASP76114:EBA4462-MON.

Family and domain databases

HAMAPMF_00186.
[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]
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...

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Entry information

Entry nameGLPK_AZOSE
AccessionPrimary (citable) accession number: Q5P212
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 4, 2005
Last modified: November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents