Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07874 (ALGA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alginate biosynthesis protein AlgA

Including the following 2 domains:

  1. Mannose-6-phosphate isomerase
    EC=5.3.1.8
    Alternative name(s):
    Phosphohexomutase
    Phosphomannose isomerase
    Short name=PMI
  2. Mannose-1-phosphate guanylyltransferase
    EC=2.7.7.13
    Alternative name(s):
    GDP-mannose pyrophosphorylase
    Short name=GMP
    Short name=GMPP
    GTP--mannose-1-phosphate guanylyltransferase
Gene names
Name:algA
Synonyms:pmi
Ordered Locus Names:PA3551
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces a precursor for alginate polymerization. The alginate layer provides a protective barrier against host immune defenses and antibiotics. Ref.3

Catalytic activity

D-mannose 6-phosphate = D-fructose 6-phosphate. Ref.3

GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose. Ref.3

Cofactor

Cobalt (for PMI). Ref.3

Pathway

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.

Subunit structure

Monomer. Ref.3

Sequence similarities

Belongs to the mannose-6-phosphate isomerase type 2 family.

Biophysicochemical properties

Kinetic parameters:

KM=3.03 mM for D-mannose 6-phosphate Ref.3

KM=20.5 µM for D-mannose 1-phosphate

KM=29.5 µM for GTP

KM=14.2 µM for GDP-D-mannose

Vmax=830 nmol/min/mg enzyme for the PMI forward reaction

Vmax=5680 nmol/min/mg enzyme for the GMP forward reaction

Vmax=5170 nmol/min/mg enzyme for the GMP reverse reaction

pH dependence:

Optimum pH is 7.0 for PMI activity, and 7.6 for GMP activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Alginate biosynthesis protein AlgA
PRO_0000194248

Experimental info

Sequence conflict26 – 272FL → LV in AAA25972. Ref.1
Sequence conflict1151I → L in AAA25972. Ref.1
Sequence conflict1571S → T in AAA25972. Ref.1
Sequence conflict359 – 3602EV → DL in AAA25972. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P07874 [UniParc].

Last modified January 11, 2001. Version 3.
Checksum: 2D497AF9059AEF97

FASTA48153,128
        10         20         30         40         50         60 
MIPVILSGGS GSRLWPLSRK QYPKQFLALT GDDTLFQQTI KRLAFDGMQA PLLVCNKEHR 

        70         80         90        100        110        120 
FIVQEQLEAQ NLASQAILLE PFGRNTAPAV AIAAMKLVAE GRDELLLILP ADHVIEDQRA 

       130        140        150        160        170        180 
FQQALALATN AAEKGEMVLF GIPASRPETG YGYIRASADA QLPEGVSRVQ SFVEKPDEAR 

       190        200        210        220        230        240 
AREFVAAGGY YWNSGMFLFR ASRYLEELKK HDADIYDTCL LALERSQHDG DLVNIDAATF 

       250        260        270        280        290        300 
ECCPDNSIDY AVMEKTSRAC VVPLSAGWND VGSWSSIWDV HAKDANGNVT KGDVLVHDSH 

       310        320        330        340        350        360 
NCLVHGNGKL VSVIGLEDIV VVETKDAMMI AHKDRVQDVK HVVKDLDAQG RSETQNHCEV 

       370        380        390        400        410        420 
YRPWGSYDSV DMGGRFQVKH ITVKPGARLS LQMHHHRAEH WIVVSGTAQV TCDDKTFLLT 

       430        440        450        460        470        480 
ENQSTYIPIA SVHRLANPGK IPLEIIEVQS GSYLGEDDIE RLEDVYGRTA EPALQVVAGS 


R 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence analysis of the phosphomannose isomerase gene (pmi) of Pseudomonas aeruginosa and comparison with the corresponding Escherichia coli gene manA."
Darzins A., Frantz B., Vanags R.I., Chakrabarty A.M.
Gene 42:293-302(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]"Purification and characterization of phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa."
Shinabarger D., Berry A., May T.B., Rothmel R., Fialho A., Chakrabarty A.M.
J. Biol. Chem. 266:2080-2088(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14037 Genomic DNA. Translation: AAA25972.1.
AE004091 Genomic DNA. Translation: AAG06939.1.
PIRA38598.
B83201.
RefSeqNP_252241.1. NC_002516.2.

3D structure databases

ProteinModelPortalP07874.
SMRP07874. Positions 1-346, 371-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA3551.

Proteomic databases

PRIDEP07874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID879142.
KEGGpae:PA3551.
PATRIC19841717. VBIPseAer58763_3716.

Organism-specific databases

PseudoCAPPA3551.

Phylogenomic databases

eggNOGCOG0662.
HOGENOMHOG000153549.
KOK16011.
OMAEPSIYEN.
OrthoDBEOG6X3W6T.
ProtClustDBCLSK868066.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13384.
BRENDA2.7.7.13. 5087.
SABIO-RKP07874.
UniPathwayUPA00126; UER00423.
UPA00126; UER00930.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR006375. Man1P_GuaTrfase/Man6P_Isoase.
IPR001538. Man6P_isomerase-2_C.
IPR005835. NTP_transferase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF01050. MannoseP_isomer. 1 hit.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
TIGRFAMsTIGR01479. GMP_PMI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALGA_PSEAE
AccessionPrimary (citable) accession number: P07874
Secondary accession number(s): Q9HY66
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 115 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways