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Protein

Poly(beta-D-mannuronate) C5 epimerase

Gene

algG

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional protein that converts poly(beta-D-mannuronate) to alpha-L-guluronate and that is also part of a periplasmic protein complex that serves as a scaffold that leads the newly formed alginate polymer through the periplasmic space to the outer membrane secretin AlgE.

Pathwayi: alginate biosynthesis

This protein is involved in the pathway alginate biosynthesis, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway alginate biosynthesis and in Glycan biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • alginic acid biosynthetic process Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Alginate biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00286.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(beta-D-mannuronate) C5 epimerase (EC:5.1.3.-)
Gene namesi
Name:algG
Ordered Locus Names:PA3545
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3545.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi272 – 2721S → N: Loss of epimerase function; still capable of protecting the polymer from AlgL lyase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence analysisAdd
BLAST
Chaini36 – 543508Poly(beta-D-mannuronate) C5 epimerasePRO_0000001125Add
BLAST

Proteomic databases

PaxDbiQ51371.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA3545.

Structurei

3D structure databases

ProteinModelPortaliQ51371.
SMRiQ51371. Positions 80-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati243 – 27028PbH1 1Add
BLAST
Repeati283 – 30422PbH1 2Add
BLAST
Repeati305 – 32723PbH1 3Add
BLAST
Repeati329 – 35224PbH1 4Add
BLAST
Repeati354 – 37623PbH1 5Add
BLAST
Repeati378 – 40023PbH1 6Add
BLAST
Repeati401 – 42323PbH1 7Add
BLAST

Sequence similaritiesi

Belongs to the D-mannuronate C5-epimerase family.Curated
Contains 7 PbH1 repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4108C0K. Bacteria.
ENOG41101XF. LUCA.
HOGENOMiHOG000270136.
InParanoidiQ51371.
KOiK01795.
OMAiHDRSHGL.
OrthoDBiEOG6D5FZ4.

Family and domain databases

Gene3Di2.160.20.10. 2 hits.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR007742. NosD_dom.
IPR022441. Para_beta_helix_rpt-2.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF05048. NosD. 1 hit.
[Graphical view]
SMARTiSM00722. CASH. 1 hit.
SM00710. PbH1. 7 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR03804. para_beta_helix. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q51371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDISLSIPR RRLPRLRPLA AAVLGAVLLH GQAWAAQPVE KPQPVPAQAG
60 70 80 90 100
NEPGLTQGLK ETGNYTVTTA PAEPLHLDPP KLPDLSGYTA AAVEAKIVRK
110 120 130 140 150
PGGRASVQRM VQQQPLKEFT GGSNRLAEWV KRQRQMPQAI FIEGGYVNLA
160 170 180 190 200
QLAGKLPASA LEQVEPGVFV ARLPIVVSQG ATLDIDKQVK ELRLSQERGA
210 220 230 240 250
FLVNDGMLFV RDSKVTGWSE SKKEPAWFKT PNEFRPFLIS WGGAEVYLSN
260 270 280 290 300
STFTSFGYNA SKAYGISISQ YSPGMDKQMK RPRPKGWVID STIVDSWYGF
310 320 330 340 350
YCYEADDLVV KGNTYRDNIV YGIDPHDRSH RLIIADNTVH GTRKKHGIIV
360 370 380 390 400
SREVNDSFIF NNRSYENKLS GIVLDRNSEG NLVAYNEVYR NHSDGITLYE
410 420 430 440 450
SGDNLLWGNQ VLANRRHGIR VRNSVNIRLY ENLAAGNQLI GVYGHIKDLT
460 470 480 490 500
NTDRNIALDP FDTKVSLIVV GGKLAGNGSG PLSVDSPLSL ELYRVAMLAP
510 520 530 540
TKSSGISLPG VLGEKQDQIL DLLVRQDKAV LIDPVESQAE LQD
Length:543
Mass (Da):59,802
Last modified:November 1, 1996 - v1
Checksum:iBCB1378EC4BB4192
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27829 Genomic DNA. Translation: AAA91125.1.
AE004091 Genomic DNA. Translation: AAG06933.1.
PIRiF83202.
RefSeqiNP_252235.1. NC_002516.2.
WP_003110465.1. NZ_ASJY01000573.1.

Genome annotation databases

EnsemblBacteriaiAAG06933; AAG06933; PA3545.
GeneIDi879839.
KEGGipae:PA3545.
PATRICi19841703. VBIPseAer58763_3709.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27829 Genomic DNA. Translation: AAA91125.1.
AE004091 Genomic DNA. Translation: AAG06933.1.
PIRiF83202.
RefSeqiNP_252235.1. NC_002516.2.
WP_003110465.1. NZ_ASJY01000573.1.

3D structure databases

ProteinModelPortaliQ51371.
SMRiQ51371. Positions 80-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3545.

Proteomic databases

PaxDbiQ51371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06933; AAG06933; PA3545.
GeneIDi879839.
KEGGipae:PA3545.
PATRICi19841703. VBIPseAer58763_3709.

Organism-specific databases

PseudoCAPiPA3545.

Phylogenomic databases

eggNOGiENOG4108C0K. Bacteria.
ENOG41101XF. LUCA.
HOGENOMiHOG000270136.
InParanoidiQ51371.
KOiK01795.
OMAiHDRSHGL.
OrthoDBiEOG6D5FZ4.

Enzyme and pathway databases

UniPathwayiUPA00286.

Family and domain databases

Gene3Di2.160.20.10. 2 hits.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR007742. NosD_dom.
IPR022441. Para_beta_helix_rpt-2.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF05048. NosD. 1 hit.
[Graphical view]
SMARTiSM00722. CASH. 1 hit.
SM00710. PbH1. 7 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR03804. para_beta_helix. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pseudomonas aeruginosa AlgG is a polymer level alginate C5-mannuronan epimerase."
    Franklin M.J., Chitnis C.E., Gacesa P., Sonesson A., White D.C., Ohman D.E.
    J. Bacteriol. 176:1821-1830(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FRD1.
  2. "Alginate synthesis in Pseudomonas aeruginosa: the role of AlgL (alginate lyase) and AlgX."
    Monday S.R., Schiller N.L.
    J. Bacteriol. 178:625-632(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FRD1.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  4. "The dual roles of AlgG in C-5-epimerization and secretion of alginate polymers in Pseudomonas aeruginosa."
    Jain S., Franklin M.J., Ertesvaag H., Valla S., Ohman D.E.
    Mol. Microbiol. 47:1123-1133(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF SER-272.

Entry informationi

Entry nameiALGG_PSEAE
AccessioniPrimary (citable) accession number: Q51371
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.