Reviewed, UniProtKB/Swiss-Prot P07874 (ALGA_PSEAE)

Names and origin

Protein names

Recommended name:
    Alginate biosynthesis protein algA
Including the following 2 domains:
    1- Recommended name:
            Mannose-6-phosphate isomerase
              EC=5.3.1.8
        Alternative name(s):
            Phosphomannose isomerase
              Short name=PMI
            Phosphohexomutase
    2- Recommended name:
            Mannose-1-phosphate guanylyltransferase
              EC=2.7.7.13
        Alternative name(s):
            GDP-mannose pyrophosphorylase
              Short name=GMPP
              Short name=GMP
            GTP--mannose-1-phosphate guanylyltransferase

Gene names

Name:	algA
Synonyms:	pmi
Ordered Locus Names:	PA3551

Organism

Pseudomonas aeruginosa [Complete proteome] [HAMAP]

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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-D-mannose biosynthesis; GDP-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1. Nucleotide-sugar biosynthesis; GDP-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 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.

Ontologies

Keywords
Biological process	Alginate biosynthesis
Ligand	Cobalt GTP-binding Nucleotide-binding
Molecular function	Isomerase Nucleotidyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	alginic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW mannose-1-phosphate guanylyltransferase activity Inferred from electronic annotation. Source: EC mannose-6-phosphate isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	Alginate biosynthesis protein algA		PRO_0000194248
Experimental info
	Sequence conflict	26 – 27	2	FL → LV in AAA25972. Ref.1
	Sequence conflict	115	1	I → L in AAA25972. Ref.1
	Sequence conflict	157	1	S → T in AAA25972. Ref.1
	Sequence conflict	359 – 360	2	EV → DL in AAA25972. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07874-1 [UniParc]. Last modified January 11, 2001. Version 3. Checksum: 2D497AF9059AEF97	FASTA	481	53,128
	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

References

	« Hide 'large scale' referencesShow '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: 3089876] [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. , 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: 10984043] [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: 1846611] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M14037 Genomic DNA. Translation: AAA25972.1. AE004091 Genomic DNA. Translation: AAG06939.1.
PIR	A38598. B83201.
RefSeq	NP_252241.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	879142.
GenomeReviews	Gene locus PA3551 in contig AE004091_GR.
KEGG	pae:PA3551.
Organism-specific databases
PseudoCAP	PA3551.
CMR	Search...
Phylogenomic databases
HOGENOM	P07874.
OMA	P07874. AEHRMVA.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13384. PAER208964:PA3551-MON.
BRENDA	2.7.7.13. 354. 2.7.7.22. 354. 5.3.1.8. 354.
Family and domain databases
InterPro	IPR006375. Man1P_GuaTrfase/Man6P_Isoase. IPR001538. Man6P_isomerase-2_C. IPR005835. NTP_transferase. IPR014710. RmlC-like_jellyroll. [Graphical view]
Gene3D	G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
Pfam	PF01050. MannoseP_isomer. 1 hit. PF00483. NTP_transferase. 1 hit. [Graphical view]
ProDom	PD002664. Man6P_isomerII. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01479. GMP_PMI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALGA_PSEAE

Accession

Primary (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:	June 16, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)