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Protein

Phosphomannomutase/phosphoglucomutase

Gene

algC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Highly reversible phosphoryltransferase. 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 lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625).10 Publications

Catalytic activityi

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.1 Publication
Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg(2+) ion per subunit (PubMed:23517223). Zn2+ can substitute, but yields a catalytically inactive enzyme (PubMed:14725765, PubMed:16880541, PubMed:16595672).1 Publication3 Publications

Enzyme regulationi

Both activities are stimulated by EDTA and Mg2+, the dual presence of Mg2+ and another divalent cation inhibits both activities. Requires glucose 1,6-bisphosphate (G1,6P) as an activator (PubMed:8050998, PubMed:11716469). Reaction making glucose 6-phosphate is subject to substrate inhibition, reactions making mannose 1-phosphate or glucose 1-phosphate are not. 1-deoxyglucose 6-phosphate competitively inhibits glucose 1-phosphate (PubMed:11716469). Inhibited by xylose 1-phosphate (PubMed:16880541).2 Publications1 Publication

Kineticsi

kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1) for mannose 1-phosphate.1 Publication

  1. KM=22 µM for glucose 1-phosphate1 Publication
  2. KM=17 µM for mannose 1-phosphate1 Publication
  3. KM=5.4 µM for glucose 1-phosphate1 Publication
  4. KM=0.38 mM for glucose 6-phosphate1 Publication
  5. KM=0.51 mM for mannose 6-phosphate1 Publication
  6. KM=27.3 µM for glucose 6-phosphate1 Publication

Temperature dependencei

TM is 66 degrees Celsius for phosphorylated protein and 62 degrees Celsius for unphosphorylated protein.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei17 – 171Substrate phosphate group4 Publications
Active sitei20 – 201Proton donor1 Publication
Active sitei108 – 1081Non-phosphorylated intermediate3 Publications
Metal bindingi108 – 1081Magnesium; via phosphate group6 Publications
Metal bindingi242 – 2421Magnesium8 Publications
Metal bindingi244 – 2441Magnesium8 Publications
Metal bindingi246 – 2461Magnesium8 Publications
Binding sitei285 – 2851Substrate sugar group2 Publications
Binding sitei308 – 3081Substrate sugar group4 Publications
Active sitei329 – 3291Proton acceptor1 Publication

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB
  2. phosphoglucomutase activity Source: UniProtKB
  3. phosphomannomutase activity Source: UniProtKB

GO - Biological processi

  1. alginic acid biosynthetic process Source: PseudoCAP
  2. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  3. lipopolysaccharide core region biosynthetic process Source: PseudoCAP
  4. O antigen biosynthetic process Source: CACAO
  5. pathogenesis Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Alginate biosynthesis, Lipopolysaccharide biosynthesis, Virulence

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKP26276.
UniPathwayiUPA00030.
UPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase/phosphoglucomutase (EC:5.4.2.21 Publication, EC:5.4.2.81 Publication)
Short name:
PMM / PGM
Gene namesi
Name:algC
Ordered Locus Names:PA5322
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA5322.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

No longer expresses O-antigen LPS side chain or A-band LPS, sensitive to serum, resistant to virus E79. Has no phosphomannomutase nor phosphoglucomutase activites (PubMed:7515870, PubMed:8050998). Does not make rhamnolipid (PubMed:10481091).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151R → A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold. 1 Publication
Mutagenesisi20 – 201R → A: No phosphoglucomutase activity. 1 Publication
Mutagenesisi108 – 1081S → A or V: About 5% activity, still subject to substrate inhibition and requires G1,6P as an activator; phosphorylation occurs at a different site. 1 Publication
Mutagenesisi108 – 1081S → C: KM for G1P unchanged, kcat decreases 24-fold; G1,6P stimulates reaction by 2-3 orders of magnitude. No stable protein phosphorylation detected, altered ligation of metal residue. 1 Publication
Mutagenesisi110 – 1101N → A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold. 1 Publication
Mutagenesisi247 – 2471R → A: Small reduction in KM, small increase in dissociation of G1,6P intermediate. 1 Publication
Mutagenesisi262 – 2621R → A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region. 1 Publication
Mutagenesisi325 – 3251E → A: Reduces KM and Vmax approximately 2-fold. 1 Publication
Mutagenesisi329 – 3291H → A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure. 1 Publication
Mutagenesisi368 – 3681P → G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact. 1 Publication
Mutagenesisi421 – 4211R → C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 463462Phosphomannomutase/phosphoglucomutasePRO_0000147814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Expressioni

Inductioni

By D-mannose 6-phosphate.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5322.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Beta strandi16 – 238Combined sources
Turni24 – 263Combined sources
Helixi29 – 4517Combined sources
Beta strandi50 – 556Combined sources
Helixi61 – 7313Combined sources
Turni74 – 763Combined sources
Beta strandi78 – 847Combined sources
Helixi87 – 9610Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi114 – 1218Combined sources
Helixi129 – 14012Combined sources
Beta strandi149 – 1524Combined sources
Helixi156 – 1649Combined sources
Beta strandi173 – 1786Combined sources
Helixi183 – 1864Combined sources
Helixi188 – 1969Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi211 – 2133Combined sources
Helixi220 – 2234Combined sources
Helixi224 – 2329Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi245 – 2528Combined sources
Helixi260 – 27415Combined sources
Beta strandi279 – 2835Combined sources
Helixi289 – 2968Combined sources
Beta strandi300 – 3045Combined sources
Helixi308 – 31811Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi328 – 3325Combined sources
Turni333 – 3364Combined sources
Beta strandi338 – 3403Combined sources
Helixi342 – 35413Combined sources
Beta strandi356 – 3583Combined sources
Helixi360 – 3656Combined sources
Beta strandi376 – 3794Combined sources
Turni382 – 3843Combined sources
Helixi385 – 39511Combined sources
Beta strandi400 – 4045Combined sources
Beta strandi406 – 4138Combined sources
Beta strandi416 – 4227Combined sources
Beta strandi424 – 43714Combined sources
Helixi438 – 45518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K2YX-ray1.75X1-463[»]
1K35X-ray2.20A1-463[»]
1P5DX-ray1.60X1-463[»]
1P5GX-ray1.61X1-463[»]
1PCJX-ray2.00X1-463[»]
1PCMX-ray1.90X1-463[»]
2FKFX-ray2.00A2-463[»]
2FKMX-ray1.90X2-463[»]
2H4LX-ray2.40X1-463[»]
2H5AX-ray1.72X1-463[»]
3BKQX-ray2.05X1-463[»]
3C04X-ray2.20A1-463[»]
3RSMX-ray2.10A1-463[»]
4IL8X-ray1.80A1-463[»]
4MRQX-ray1.90A9-463[»]
ProteinModelPortaliP26276.
SMRiP26276. Positions 9-463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26276.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 142130Topological domain 11 PublicationAdd
BLAST
Regioni159 – 25597Topological domain 21 PublicationAdd
BLAST
Regioni260 – 364105Topological domain 31 PublicationAdd
BLAST
Regioni325 – 3295Binds substrate sugar group3 Publications
Regioni375 – 45379Topological domain 41 PublicationAdd
BLAST
Regioni421 – 4255Binds substrate phosphate group3 Publications

Domaini

Consists of 4 domains; domains 1-3 have a similar toplological core while domain 4 folds over and closes the active site from a hinge region. Mutants in the hinge region (residues 262 and 368-369) generally increase KM for glucose 1-phosphate 2-fold while reducing kcat about 10-fold (PubMed:18690721).3 Publications

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268679.
InParanoidiP26276.
OMAiAWFNLRA.
OrthoDBiEOG6W9X55.
PhylomeDBiP26276.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTAKAPTLP ASIFRAYDIR GVVGDTLTAE TAYWIGRAIG SESLARGEPC
60 70 80 90 100
VAVGRDGRLS GPELVKQLIQ GLVDCGCQVS DVGMVPTPVL YYAANVLEGK
110 120 130 140 150
SGVMLTGSHN PPDYNGFKIV VAGETLANEQ IQALRERIEK NDLASGVGSV
160 170 180 190 200
EQVDILPRYF KQIRDDIAMA KPMKVVVDCG NGVAGVIAPQ LIEALGCSVI
210 220 230 240 250
PLYCEVDGNF PNHHPDPGKP ENLKDLIAKV KAENADLGLA FDGDGDRVGV
260 270 280 290 300
VTNTGTIIYP DRLLMLFAKD VVSRNPGADI IFDVKCTRRL IALISGYGGR
310 320 330 340 350
PVMWKTGHSL IKKKMKETGA LLAGEMSGHV FFKERWFGFD DGIYSAARLL
360 370 380 390 400
EILSQDQRDS EHVFSAFPSD ISTPEINITV TEDSKFAIIE ALQRDAQWGE
410 420 430 440 450
GNITTLDGVR VDYPKGWGLV RASNTTPVLV LRFEADTEEE LERIKTVFRN
460
QLKAVDSSLP VPF
Length:463
Mass (Da):50,296
Last modified:January 23, 2007 - v4
Checksum:i35EE59406379FFB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41A → V in AAA25701 (PubMed:1903398).Curated
Sequence conflicti21 – 211G → R in AAA25701 (PubMed:1903398).Curated
Sequence conflicti437 – 4371T → P in AAA25701 (PubMed:1903398).Curated

Mass spectrometryi

Molecular mass is 50220 Da from positions 2 - 463. Determined by MALDI. May be phosphorylated, protein expressed in E.coli.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60873 Genomic DNA. Translation: AAA25701.1.
AE004091 Genomic DNA. Translation: AAG08707.1.
PIRiA40013.
H82979.

Genome annotation databases

EnsemblBacteriaiAAG08707; AAG08707; PA5322.
PATRICi19845501. VBIPseAer58763_5577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60873 Genomic DNA. Translation: AAA25701.1.
AE004091 Genomic DNA. Translation: AAG08707.1.
PIRiA40013.
H82979.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K2YX-ray1.75X1-463[»]
1K35X-ray2.20A1-463[»]
1P5DX-ray1.60X1-463[»]
1P5GX-ray1.61X1-463[»]
1PCJX-ray2.00X1-463[»]
1PCMX-ray1.90X1-463[»]
2FKFX-ray2.00A2-463[»]
2FKMX-ray1.90X2-463[»]
2H4LX-ray2.40X1-463[»]
2H5AX-ray1.72X1-463[»]
3BKQX-ray2.05X1-463[»]
3C04X-ray2.20A1-463[»]
3RSMX-ray2.10A1-463[»]
4IL8X-ray1.80A1-463[»]
4MRQX-ray1.90A9-463[»]
ProteinModelPortaliP26276.
SMRiP26276. Positions 9-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5322.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08707; AAG08707; PA5322.
PATRICi19845501. VBIPseAer58763_5577.

Organism-specific databases

PseudoCAPiPA5322.

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268679.
InParanoidiP26276.
OMAiAWFNLRA.
OrthoDBiEOG6W9X55.
PhylomeDBiP26276.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00126; UER00424.
SABIO-RKP26276.

Miscellaneous databases

EvolutionaryTraceiP26276.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION AS A PHOSPHOMANNOMUTASE, MUTAGENESIS OF ARG-421.
    Strain: 8830.
  2. 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] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A PHOSPHOGLUCOMUTASE, DISRUPTION PHENOTYPE.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 and PAC1R.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
    Strain: 8830.
  5. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, POSSIBLE REACTION MECHANISM, MASS SPECTROMETRY, PHOSPHORYLATION, 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH METAL OF WILD-TYPE AND ASP-108 MUTANT, DOMAIN, ACTIVE SITE, PHOSPHORYLATION AT SER-108.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  8. "Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa."
    Regni C., Naught L., Tipton P.A., Beamer L.J.
    Structure 12:55-63(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH METAL AND SUBSTRATES, COFACTOR, ACTIVE SITE, PHOSPHORYLATION AT SER-108, MUTAGENESIS OF GLU-325.
  9. "Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor."
    Regni C., Shackelford G.S., Beamer L.J.
    Acta Crystallogr. F 62:722-726(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH METAL AND SUBSTRATE OR INHIBITOR, FUNCTION, COFACTOR, ENZYME REGULATION, ACTIVE SITE, PHOSPHORYLATION AT SER-108.
  10. "The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme."
    Regni C., Schramm A.M., Beamer L.J.
    J. Biol. Chem. 281:15564-15571(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-463 IN COMPLEX WITH METAL AND REACTION INTERMEDIATE, FUNCTION, COFACTOR, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION AT SER-108, MUTAGENESIS OF ARG-15; ARG-20; ASN-110; ARG-247 AND ARG-421.
  11. "Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa."
    Schramm A.M., Mehra-Chaudhary R., Furdui C.M., Beamer L.J.
    Biochemistry 47:9154-9162(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF GLY-368 MUTANT IN COMPLEX WITH METAL OF APOPROTEIN AND IN COMPLEX WITH SUBSTRATE, FUNCTION, COFACTOR, DOMAIN, MUTAGENESIS OF ARG-262 AND PRO-368.
  12. "Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect."
    Sarma A.V., Anbanandam A., Kelm A., Mehra-Chaudhary R., Wei Y., Qin P., Lee Y., Berjanskii M.V., Mick J.A., Beamer L.J., Van Doren S.R.
    Biochemistry 51:807-819(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF CYS-108 MUTANT IN COMPLEX WITH METAL, FUNCTION, DOMAIN, MUTAGENESIS OF SER-108.
  13. "Identification of an essential active-site residue in the alpha-D-phosphohexomutase enzyme superfamily."
    Lee Y., Mehra-Chaudhary R., Furdui C., Beamer L.J.
    FEBS J. 280:2622-2632(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF ALA-329 MUTANT IN COMPLEX WITH MAGNESIUM, FUNCTION, COFACTOR, REACTION MECHANISM, ACTIVE SITE, MUTAGENESIS OF HIS-329.
  14. "Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase."
    Lee Y., Villar M.T., Artigues A., Beamer L.J.
    J. Biol. Chem. 289:4674-4682(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF DEPHOSPHORYLATED PROTEIN IN COMPLEX WITH METAL, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiALGC_PSEAE
AccessioniPrimary (citable) accession number: P26276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 131 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Most crystals have Zn2+ rather than Mg2+ and are catalytically inactive.3 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.