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Entry version 148 (08 May 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Phosphomannomutase/phosphoglucomutase

Gene

algC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit (PubMed:23517223). Zn2+ can substitute, but yields a catalytically inactive enzyme (PubMed:14725765, PubMed:16880541, PubMed:16595672).3 Publications1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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).1 Publication2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: GDP-alpha-D-mannose biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Alginate biosynthesis protein AlgA (algA)
    2. Phosphomannomutase/phosphoglucomutase (algC)
    This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

    Pathwayi: lipopolysaccharide biosynthesis

    This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.
    View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei17Substrate phosphate group4 Publications1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei20Proton donor1 Publication1
    Active sitei108Non-phosphorylated intermediate3 Publications1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi108Magnesium; via phosphate group6 Publications1
    Metal bindingi242Magnesium8 Publications1
    Metal bindingi244Magnesium8 Publications1
    Metal bindingi246Magnesium8 Publications1
    Binding sitei285Substrate sugar group2 Publications1
    Binding sitei308Substrate sugar group4 Publications1
    Active sitei329Proton acceptor1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionIsomerase, Multifunctional enzyme
    Biological processAlginate biosynthesis, Lipopolysaccharide biosynthesis, Virulence
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-19202

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    5.4.2.2 5087
    5.4.2.8 5087

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P26276

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00030

    UPA00126;UER00424

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Phosphomannomutase/phosphoglucomutase (EC:5.4.2.21 Publication, EC:5.4.2.81 Publication)
    Short name:
    PMM / PGM
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:algC
    Ordered Locus Names:PA5322
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri208964 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002438 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    Organism-specific databases

    Pseudomonas genome database

    More...
    PseudoCAPi
    PA5322

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi15R → A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold. 1 Publication1
    Mutagenesisi20R → A: No phosphoglucomutase activity. 1 Publication1
    Mutagenesisi108S → 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 Publication1
    Mutagenesisi108S → 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 Publication1
    Mutagenesisi110N → A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold. 1 Publication1
    Mutagenesisi247R → A: Small reduction in KM, small increase in dissociation of G1,6P intermediate. 1 Publication1
    Mutagenesisi262R → A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region. 1 Publication1
    Mutagenesisi325E → A: Reduces KM and Vmax approximately 2-fold. 1 Publication1
    Mutagenesisi329H → A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure. 1 Publication1
    Mutagenesisi368P → G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact. 1 Publication1
    Mutagenesisi421R → C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity. 2 Publications1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB02007 alpha-D-glucose 6-phosphate
    DB02843 Alpha-D-Glucose-1-Phosphate
    DB02900 alpha-D-mannose 6-phosphate
    DB02867 D-Mannose 1-Phosphate
    DB04522 Phosphonoserine

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001478142 – 463Phosphomannomutase/phosphoglucomutaseAdd BLAST462

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei108Phosphoserine4 Publications1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P26276

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P26276

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P26276

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By D-mannose 6-phosphate.

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.1 Publication

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1463
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB 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[»]

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P26276

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P26276

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni13 – 142Topological domain 11 PublicationAdd BLAST130
    Regioni159 – 255Topological domain 21 PublicationAdd BLAST97
    Regioni260 – 364Topological domain 31 PublicationAdd BLAST105
    Regioni325 – 329Binds substrate sugar group3 Publications5
    Regioni375 – 453Topological domain 41 PublicationAdd BLAST79
    Regioni421 – 425Binds substrate phosphate group3 Publications5

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4107QKV Bacteria
    COG1109 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000268679

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P26276

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    HSGEINF

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P26276

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in 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
    IPR036900 A-D-PHexomutase_C_sf
    IPR016066 A-D-PHexomutase_CS
    IPR005841 Alpha-D-phosphohexomutase_SF

    Pfam protein domain database

    More...
    Pfami
    View protein in 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

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00509 PGMPMM

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53738 SSF53738, 3 hits
    SSF55957 SSF55957, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00710 PGM_PMM, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i35EE59406379FFB8
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti4A → V in AAA25701 (PubMed:1903398).Curated1
    Sequence conflicti21G → R in AAA25701 (PubMed:1903398).Curated1
    Sequence conflicti437T → P in AAA25701 (PubMed:1903398).Curated1

    <p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>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:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    M60873 Genomic DNA Translation: AAA25701.1
    AE004091 Genomic DNA Translation: AAG08707.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A40013
    H82979

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAG08707; AAG08707; PA5322

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
    PDB 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[»]
    SMRiP26276
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    DrugBankiDB02007 alpha-D-glucose 6-phosphate
    DB02843 Alpha-D-Glucose-1-Phosphate
    DB02900 alpha-D-mannose 6-phosphate
    DB02867 D-Mannose 1-Phosphate
    DB04522 Phosphonoserine

    PTM databases

    iPTMnetiP26276

    Proteomic databases

    PaxDbiP26276
    PRIDEiP26276

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG08707; AAG08707; PA5322

    Organism-specific databases

    PseudoCAPiPA5322

    Phylogenomic databases

    eggNOGiENOG4107QKV Bacteria
    COG1109 LUCA
    HOGENOMiHOG000268679
    InParanoidiP26276
    OMAiHSGEINF
    PhylomeDBiP26276

    Enzyme and pathway databases

    UniPathwayi
    UPA00030

    UPA00126;UER00424

    BioCyciMetaCyc:MONOMER-19202
    BRENDAi5.4.2.2 5087
    5.4.2.8 5087
    SABIO-RKiP26276

    Miscellaneous databases

    EvolutionaryTraceiP26276

    Family and domain databases

    InterProiView protein in 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
    IPR036900 A-D-PHexomutase_C_sf
    IPR016066 A-D-PHexomutase_CS
    IPR005841 Alpha-D-phosphohexomutase_SF
    PfamiView protein in 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
    PRINTSiPR00509 PGMPMM
    SUPFAMiSSF53738 SSF53738, 3 hits
    SSF55957 SSF55957, 1 hit
    PROSITEiView protein in PROSITE
    PS00710 PGM_PMM, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiALGC_PSEAE
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P26276
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: May 8, 2019
    This is version 148 of the entry and version 4 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

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

    Documents

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