Reviewed, UniProtKB/Swiss-Prot P26276 (ALGC_PSEAE)

Names and origin

Protein names

Recommended name:
    Phosphomannomutase/phosphoglucomutase
      Short name=PMM / PGM
    EC=5.4.2.8
    EC=5.4.2.2

Gene names

Name:	algC
Ordered Locus Names:	PA5322

Organism

Pseudomonas aeruginosa [Complete proteome] [HAMAP]

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The phosphomannomutase activity produces a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core-LPS biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity, and for biofilm production. Ref.3 Ref.4
Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit.
Pathway	Nucleotide-sugar biosynthesis; GDP-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subunit structure	Monomer.
Induction	By D-mannose 6-phosphate.
Sequence similarities	Belongs to the phosphohexose mutase family.
Mass spectrometry	Molecular mass is 50220 Da from positions 2 - 463. Determined by MALDI. Ref.6

Ontologies

Keywords
Biological process	Alginate biosynthesis Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	3D-structure 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: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Inferred from electronic annotation. Source: EC phosphomannomutase 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

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 463

462

Phosphomannomutase/phosphoglucomutase

PRO_0000147814

Sites

Active site

108

1

Phosphoserine intermediate

Metal binding

108

1

Magnesium; via phosphate group

Metal binding

242

1

Magnesium

Metal binding

244

1

Magnesium

Metal binding

246

1

Magnesium

Binding site

325

1

Substrate

Binding site

327

1

Substrate

Binding site

329

1

Substrate

Site

421

1

Interacts with the biphosphorylated intermediate

Experimental info

Mutagenesis

108

1

S → A or V: Decrease in activity; phosphorylation occurs at a different site. Ref.6

Mutagenesis

421

1

R → C: Loss of activity. Ref.1

Sequence conflict

4

1

A → V in AAA25701. Ref.1

Sequence conflict

21

1

G → R in AAA25701. Ref.1

Sequence conflict

437

1

T → P in AAA25701. Ref.1

Secondary structure

1

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463

Helix Strand Turn

Details...

Helix

11 – 13

3

Beta strand

16 – 23

8

Turn

24 – 26

3

Helix

29 – 45

17

Beta strand

50 – 55

6

Helix

61 – 73

13

Beta strand

78 – 84

7

Helix

87 – 96

10

Beta strand

100 – 105

6

Beta strand

114 – 121

8

Helix

129 – 139

11

Beta strand

149 – 152

4

Helix

156 – 166

11

Beta strand

174 – 178

5

Helix

183 – 186

4

Helix

188 – 194

7

Beta strand

198 – 203

6

Helix

220 – 223

4

Helix

224 – 233

10

Beta strand

236 – 241

6

Beta strand

248 – 252

5

Helix

260 – 274

15

Beta strand

279 – 283

5

Helix

288 – 296

9

Beta strand

300 – 304

5

Helix

308 – 318

11

Beta strand

321 – 324

4

Beta strand

330 – 332

3

Beta strand

338 – 340

3

Helix

342 – 354

13

Helix

360 – 365

6

Beta strand

376 – 379

4

Turn

382 – 384

3

Helix

385 – 395

11

Beta strand

400 – 404

5

Beta strand

406 – 413

8

Beta strand

416 – 422

7

Beta strand

424 – 437

14

Helix

438 – 455

18

Sequences

	Sequence		Length	Mass (Da)
	P26276-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 35EE59406379FFB8	FASTA	463	50,296
	10 20 30 40 50 60 MSTAKAPTLP ASIFRAYDIR GVVGDTLTAE TAYWIGRAIG SESLARGEPC VAVGRDGRLS 70 80 90 100 110 120 GPELVKQLIQ GLVDCGCQVS DVGMVPTPVL YYAANVLEGK SGVMLTGSHN PPDYNGFKIV 130 140 150 160 170 180 VAGETLANEQ IQALRERIEK NDLASGVGSV EQVDILPRYF KQIRDDIAMA KPMKVVVDCG 190 200 210 220 230 240 NGVAGVIAPQ LIEALGCSVI PLYCEVDGNF PNHHPDPGKP ENLKDLIAKV KAENADLGLA 250 260 270 280 290 300 FDGDGDRVGV VTNTGTIIYP DRLLMLFAKD VVSRNPGADI IFDVKCTRRL IALISGYGGR 310 320 330 340 350 360 PVMWKTGHSL IKKKMKETGA LLAGEMSGHV FFKERWFGFD DGIYSAARLL EILSQDQRDS 370 380 390 400 410 420 EHVFSAFPSD ISTPEINITV TEDSKFAIIE ALQRDAQWGE GNITTLDGVR VDYPKGWGLV 430 440 450 460 RASNTTPVLV LRFEADTEEE LERIKTVFRN QLKAVDSSLP VPF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase." Zielinski N.A., Chakrabarty A.M., Berry A. J. Biol. Chem. 266:9754-9763(1991) [PubMed: 1903398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, MUTAGENESIS OF ARG-421. Strain: 8830.
[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]	"The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core." Coyne M.J. Jr., Russell K.S., Coyle C.L., Goldberg J.B. J. Bacteriol. 176:3500-3507(1994) [PubMed: 7515870] [Abstract] Cited for: FUNCTION. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 and PAC1R.
[4]	"The Pseudomonas aeruginosa algC gene product participates in rhamnolipid biosynthesis." Olvera C., Goldberg J.B., Sanchez R., Soberon-Chavez G. FEMS Microbiol. Lett. 179:85-90(1999) [PubMed: 10481091] [Abstract] Cited for: FUNCTION. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[5]	"Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide." Ye R.W., Zielinski N.A., Chakrabarty A.M. J. Bacteriol. 176:4851-4857(1994) [PubMed: 8050998] [Abstract] Cited for: CHARACTERIZATION. Strain: 8830.
[6]	"Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase." Naught L.E., Tipton P.A. Arch. Biochem. Biophys. 396:111-118(2001) [PubMed: 11716469] [Abstract] Cited for: CHARACTERIZATION, MASS SPECTROMETRY, MUTAGENESIS OF SER-108. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[7]	"Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors." Regni C., Tipton P.A., Beamer L.J. Structure 10:269-279(2002) [PubMed: 11839312] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M60873 Genomic DNA. Translation: AAA25701.1.
AE004091 Genomic DNA. Translation: AAG08707.1.

PIR

A40013.
H82979.

RefSeq

NP_254009.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K2Y	X-ray	1.75	X	1-463	[»]
1K35	X-ray	2.20	A	1-463	[»]
1P5D	X-ray	1.60	X	1-463	[»]
1P5G	X-ray	1.61	X	1-463	[»]
1PCJ	X-ray	2.00	X	1-463	[»]
1PCM	X-ray	1.90	X	1-463	[»]
2FKF	X-ray	2.00	A	2-462	[»]
2FKM	X-ray	1.90	X	2-462	[»]
2H4L	X-ray	2.40	X	1-462	[»]
2H5A	X-ray	1.72	X	2-462	[»]
3BKQ	X-ray	2.05	X	1-463	[»]
3C04	X-ray	2.20	A	1-463	[»]

ModBase

Search...

Genome annotation databases

GeneID

879406.

GenomeReviews

Gene locus PA5322 in contig AE004091_GR.

KEGG

pae:PA5322.

Organism-specific databases

PseudoCAP

PA5322.

CMR

Search...

Phylogenomic databases

HOGENOM

P26276.

OMA

P26276. ARPMKIV.

Enzyme and pathway databases

BioCyc

PAER208964:PA5322-MON.

BRENDA

5.4.2.2. 354.
5.4.2.8. 354.

Family and domain databases

InterPro

IPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. A-D-PHexomutase_N.
[Graphical view]

Gene3D

G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.

Pfam

PF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]

PRINTS

PR00509. PGMPMM.

PROSITE

PS00710. PGM_PMM. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ALGC_PSEAE

Accession

Primary (citable) accession number: P26276

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 87 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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