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P23536 (PT1_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate-protein phosphotransferase
EC=2.7.3.9
Alternative name(s):
Phosphotransferase system, enzyme I
Short name=Protein I
Gene names
Name:phbI
Synonyms:ptsI
Ordered Locus Names:H16_A0326
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).

Catalytic activity

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Cofactor

Magnesium By similarity.

Subcellular location

Cytoplasm.

Domain

The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 586586Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147053

Sites

Active site2011Tele-phosphohistidine intermediate By similarity
Active site5171Proton donor By similarity
Metal binding4461Magnesium By similarity
Metal binding4701Magnesium By similarity
Binding site3081Substrate By similarity
Binding site3451Substrate By similarity
Binding site4461Substrate By similarity
Binding site4671Substrate; via carbonyl oxygen By similarity
Binding site4681Substrate; via amide nitrogen By similarity
Binding site4691Substrate By similarity
Binding site4701Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict1161R → H in AAA21978. Ref.1
Sequence conflict5291L → R in AAA21978. Ref.1
Sequence conflict578 – 5869AALRQLARP → RPLRSWHDPEAIRVF in AAA21978. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23536 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1F52C8FC0A406641

FASTA58664,300
        10         20         30         40         50         60 
MPFALHGIPV SRGVAIGRAH LLAPAALDVS HYLVDEDQLD AEVERLRAAR AAVRAELAAL 

        70         80         90        100        110        120 
KRDLPRDAPE ELGAFLDVHA MILDDEALAR EPEALIRGRR YNAEWALTTR LEELMRQFDE 

       130        140        150        160        170        180 
IEDEYLRERK TDIRQVVERI LKALAGAPVL VPAPVPALAA DGEAATGVIV VAHDIAPADM 

       190        200        210        220        230        240 
LQFRHTVFHG FVTDMGGRTS HTAIVARSLD IPAAVGVQSA SELIRQDDWI IIDGDAGLVI 

       250        260        270        280        290        300 
VDPTAIILEE YRHRQSERAL EKKRLQRLRH TPAVTLDGLE IDLLANIEMA EDAGAALAAG 

       310        320        330        340        350        360 
AVGVGLFRSE FLFMNRRDEL PGEDEQFQAY RGAVDAMHGL PVTIRTIDIG ADKPLDARGD 

       370        380        390        400        410        420 
EFETALNPAL GLRAIRWSLS EPGMFLTQLR ALLRASAFGP VRLLVPMLAH ASEIDQTLAL 

       430        440        450        460        470        480 
IAKAKRQLDE RGEAYDPGMK VGAMIEIPAA VLLLPLFLRK MDFLSIGTND LIQYTLAIDR 

       490        500        510        520        530        540 
ADNAVAHLFD PLHPAVLQLV ARTIREANRA GVPVAVCGEM AGDPSMTRLL LGMGLREFSM 

       550        560        570        580 
HPAQLLRVKQ EILHAHCERL EPLVDQVLQA FDPEEQAAAL RQLARP

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of two Alcaligenes eutrophus gene loci relevant to the poly(beta-hydroxybutyric acid)-leaky phenotype which exhibit homology to ptsH and ptsI of Escherichia coli."
Pries A., Priefert H., Krueger N., Steinbuechel A.
J. Bacteriol. 173:5843-5853(1991) [PubMed: 1653223] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M69036 Genomic DNA. Translation: AAA21978.1.
AM260479 Genomic DNA. Translation: CAJ91477.1.
PIRB38120.
RefSeqYP_724845.1. NC_008313.1.

3D structure databases

ProteinModelPortalP23536.
ModBaseSearch...

Protein-protein interaction databases

STRINGP23536.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4249636.
GenomeReviewsGene locus H16_A0326 in contig AM260479_GR.
KEGGreh:H16_A0326.
PATRIC35230037. VBIRalEut6770_0689.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1080.
HOGENOMHBG456539.
OMAHRQSERA.
PhylomeDBP23536.
ProtClustDBCLSK896538.

Enzyme and pathway databases

BioCycREUT381666:H16_A0326-MONOMER.

Family and domain databases

InterProIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_enz_I.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK08483.
PANTHERPTHR22931:SF10. PTHR22931:SF10. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFPIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePT1_CUPNH
AccessionPrimary (citable) accession number: P23536
Secondary accession number(s): Q0KEU4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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