Mannose-6-phosphate isomerase
     (EC 5.3.1.8)
     (Phosphomannose isomerase)
     (PMI)
     (Phosphohexomutase)
Mannose-1-phosphate guanylyltransferase
     (EC 2.7.7.13)
     (GDP-mannose pyrophosphorylase)
     (GMPP)
     (GMP)
     (GTP--mannose-1-phosphate guanylyltransferase)

Gene name

	Name:	algA
	Synonyms:	pmi
	OrderedLocusNames:	PA3551

From

Pseudomonas aeruginosa

[TaxID: 287]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(86)90233-7; PubMed=3089876 [NCBI, ExPASy, EBI, Israel, Japan] Darzins A., Frantz B., Vanags R.I., Chakrabarty A.M.; "Nucleotide sequence analysis of the phosphomannose isomerase gene (pmi) of Pseudomonas aeruginosa and comparison with the corresponding Escherichia coli gene manA."; Gene 42:293-302(1986).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."; Nature 406:959-964(2000).
[3]	PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. PubMed=1846611 [NCBI, ExPASy, EBI, Israel, Japan] Shinabarger D., Berry A., May T.B., Rothmel R., Fialho A., Chakrabarty A.M.; "Purification and characterization of phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa."; J. Biol. Chem. 266:2080-2088(1991).

Comments

FUNCTION: Produces a precursor for alginate polymerization. The alginate layer provides a protective barrier against host immune defenses and antibiotics.
CATALYTIC ACTIVITY: D-mannose 6-phosphate = D-fructose 6-phosphate.
CATALYTIC ACTIVITY: GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.
COFACTOR: Cobalt (for PMI).

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=3.03 mM for D-mannose 6-phosphate;
	K_M=20.5 µM for D-mannose 1-phosphate;
	K_M=29.5 µM for GTP;
	K_M=14.2 µM for GDP-D-mannose;
	V_max=830 nmol/min/mg enzyme for the PMI forward reaction;
	V_max=5680 nmol/min/mg enzyme for the GMP forward reaction;
	V_max=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;

PATHWAY: Glycan biosynthesis; alginate biosynthesis; GDP-D-mannuronate from D-fructose 6-phosphate: step 1/4 .
PATHWAY: Glycan biosynthesis; alginate biosynthesis; GDP-D-mannuronate from D-fructose 6-phosphate: step 3/4 .
SUBUNIT: Monomer.
SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M14037; AAA25972.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG06939.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A38598; A38598.
B83201; B83201.

RefSeq

NP_252241.1; -.

3D structure databases

ModBase

P07874.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13384; -.
PAER208964:PA3551-MON; -.

Organism-specific databases

PseudoCAP

PA3551; -.

Ontologies

GO:0050897;	Molecular function: cobalt ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004475;	Molecular function: mannose-1-phosphate guanylyltransferase activity (inferred from electronic annotation from EC).
GO:0004476;	Molecular function: mannose-6-phosphate isomerase activity (inferred from electronic annotation from EC).
GO:0042121;	Biological process: alginic acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009103;	Biological process: lipopolysaccharide biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006375; Man1P_GuanlTrfase/Man6P_Isoase.
IPR001538; Man6P_isomerase-2_C.
IPR005835; NTP_transferase.
IPR014710; RmlC-like_jellyroll.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.

Pfam

PF01050; MannoseP_isomer; 1.
PF00483; NTP_transferase; 1.
Pfam graphical view of domain structure.

ProDom

PD002664; Man6P_isomerII; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01479; GMP_PMI; 1.

Genome annotation databases

GeneID

879142; -.

GenomeReviews

AE004091_GR; PA3551.

KEGG

pae:PA3551; -.

Phylogenomic databases

HOGENOM

P07874; -.

Genome annotation databases

CMR

P07874; PA3551.

Other

ProtoNet

P07874.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alginate biosynthesis; Cobalt; Complete proteome; Direct protein sequencing; Isomerase; Multifunctional enzyme; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 481`	`481`	`Alginate biosynthesis protein algA.`	`PRO_0000194248`
`CONFLICT`	`26 27`		`FL -> LV (in Ref. 1; AAA25972).`
`CONFLICT`	`115 115`		`I -> L (in Ref. 1; AAA25972).`
`CONFLICT`	`157 157`		`S -> T (in Ref. 1; AAA25972).`
`CONFLICT`	`359 360`		`EV -> DL (in Ref. 1; AAA25972).`

Sequence information

Length: 481 AA [This is the length of the unprocessed precursor]

Molecular weight: 53128 Da [This is the MW of the unprocessed precursor]

CRC64: 2D497AF9059AEF97 [This is a checksum on the sequence]

        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

P07874 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools