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
	OrderedLocusNames:	PP_1277

From

Pseudomonas putida (strain KT2440)

[TaxID: 160488]

[HAMAP proteome]

Taxonomy

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

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1046/j.1462-2920.2002.00366.x; PubMed=12534463 [NCBI, ExPASy, EBI, Israel, Japan]
Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
"Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440.";
Environ. Microbiol. 4:799-808(2002).

Comments

FUNCTION: Produces a precursor for alginate polymerization. The alginate layer provides a protective barrier against host immune defenses and antibiotics (By similarity).
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) (By similarity).
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 (By similarity).
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

AE015451; AAN66901.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_743437.1; -.

3D structure databases

ModBase

Q88ND5.

Enzyme and pathway databases

BioCyc

PPUT160488:PP_1277-MON; -.

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

1043792; -.

GenomeReviews

AE015451_GR; PP_1277.

KEGG

ppu:PP_1277; -.

NMPDR

fig|160488.1.peg.1267; -.

TIGR

PP_1277; -.

Phylogenomic databases

HOGENOM

Q88ND5; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 485`	`485`		`Alginate biosynthesis protein algA.`	`PRO_0000194250`

Sequence information

Length: 485 AA [This is the length of the unprocessed precursor]

Molecular weight: 53896 Da [This is the MW of the unprocessed precursor]

CRC64: 81668C8ED0E2A90C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMIPVILSGG SGSRLWPLSR KQFPKQFLAL TGEHTLFQQT IERLVFEGMD TPIVVCNKDH 

        70         80         90        100        110        120 
KFIVQEQLAA LKLETQGILM EPFGRNTAPA VAMAAMKLVN EGRDELMLVL PADHVIDDQK 

       130        140        150        160        170        180 
ALQRALALAT VAAERGEMVL FGVPATKPET GYGYIRSSQD ALLPEGVARV AQFVEKPDEK 

       190        200        210        220        230        240 
RAAEFVQAGG YFWNSGMFLF RASRFLEELK KHDGDIYDTC VLALERSQED GDVLSIDEAT 

       250        260        270        280        290        300 
FACCPDNSID YAVMEKTQRA CVVPMSAGWS DVGCWSSLWE VHEKDDNGNV TKGDVVVQDS 

       310        320        330        340        350        360 
RNCMIHGNGK LVSVIGLENI VVVETKDAMM IAHKDKVQGV KQMVKTLDEQ GRTETQNHLE 

       370        380        390        400        410        420 
VYRPWGSYDS VDMGGRFQVK HITVKPGASL SLQMHHHRAE HWIVVSGTAE VTCDENVFLL 

       430        440        450        460        470        480 
TENQSTYIPI ASVHRLRNPG KIPLEIIEVQ SGSYLGEDDI ERFEDVYGRT STPIERGVSV 


KTIAQ

Q88ND5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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