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Protein

Polyphosphate glucokinase

Gene

ppgK

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor.By similarity

Catalytic activityi

(Phosphate)(n) + D-glucose = (phosphate)(n-1) + D-glucose 6-phosphate.By similarity
ATP + D-glucose = ADP + D-glucose 6-phosphate.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi83 – 88ATPSequence analysis6

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphosphate glucokinase (EC:2.7.1.63)
Alternative name(s):
ATP-dependent glucokinase (EC:2.7.1.2)
Polyphosphate--glucose phosphotransferase
Gene namesi
Name:ppgK
Ordered Locus Names:ML1023
ORF Names:u1764fg
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML1023.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000585351 – 324Polyphosphate glucokinaseAdd BLAST324

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi272631.ML1023.

Structurei

3D structure databases

ProteinModelPortaliQ49988.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ROK (NagC/XylR) family.Curated

Phylogenomic databases

eggNOGiENOG4105DFK. Bacteria.
COG1940. LUCA.
HOGENOMiHOG000150086.
KOiK00886.
OMAiHVEMLFS.
OrthoDBiPOG091H0844.

Family and domain databases

InterProiIPR000600. ROK.
[Graphical view]
PfamiPF00480. ROK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q49988-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRLRSAAAR DRCQVLSLAY RITVAGRCQT VSPHHRQAKV SEQPSLAKEI
60 70 80 90 100
AITSTDATAD TPRTSPPSDT AGTTSRHRGF GIDIGGSSIK GGIVDLDIGQ
110 120 130 140 150
LIGDRIKLLT PQPATPLAVA KTIAEVVNAF GWTAPLGVTY PGVVTQGVVR
160 170 180 190 200
TAANVDDSWI GTNARDIISA ELNSQEVTIL NDADAAGLAE GRYGAGKNNS
210 220 230 240 250
GLIVLLTFGT GIGSAVIHNG KLIPNTEFGH LEVDGKEAEQ RAASSVKDKY
260 270 280 290 300
KWSYRTWAKQ VTRVLVAIEN AMCPDLFIAG GGISRKADRW IPLLENRTPM
310 320
VAAALQNTAG IVGAAMASTA DVTH
Length:324
Mass (Da):34,102
Last modified:November 1, 1996 - v1
Checksum:i563A5C63CC9EF6EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15181 Genomic DNA. Translation: AAA62940.1.
AL583920 Genomic DNA. Translation: CAC31404.1.
PIRiA87037.
RefSeqiNP_301756.1. NC_002677.1.
WP_010908080.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31404; CAC31404; CAC31404.
GeneIDi910085.
KEGGimle:ML1023.
PATRICi18053814. VBIMycLep78757_1852.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15181 Genomic DNA. Translation: AAA62940.1.
AL583920 Genomic DNA. Translation: CAC31404.1.
PIRiA87037.
RefSeqiNP_301756.1. NC_002677.1.
WP_010908080.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ49988.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML1023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC31404; CAC31404; CAC31404.
GeneIDi910085.
KEGGimle:ML1023.
PATRICi18053814. VBIMycLep78757_1852.

Organism-specific databases

LepromaiML1023.

Phylogenomic databases

eggNOGiENOG4105DFK. Bacteria.
COG1940. LUCA.
HOGENOMiHOG000150086.
KOiK00886.
OMAiHVEMLFS.
OrthoDBiPOG091H0844.

Family and domain databases

InterProiIPR000600. ROK.
[Graphical view]
PfamiPF00480. ROK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPGK_MYCLE
AccessioniPrimary (citable) accession number: Q49988
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The poly(P)- and ATP-dependent glucokinase reactions both follow an ordered Bi-Bi mechanism, with glucose being the second substrate to bind and glucose 6-phosphate being released last. The mechanism of poly(P) utilization is not strictly processive and is most likely nonprocessive, where there is dissociation of poly(P) prior to complete utilization.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.