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Protein

Poly(beta-D-mannuronate) C5 epimerase

Gene

algG

Organism
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Status
Reviewed-Annotation score: Annotation score: 2 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.By similarity

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

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:PSPTO_1238
OrganismiPseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Taxonomic identifieri223283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002515 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
ChainiPRO_000000112837 – 536Poly(beta-D-mannuronate) C5 epimeraseAdd BLAST500

Interactioni

Protein-protein interaction databases

STRINGi223283.PSPTO_1238.

Structurei

Secondary structure

1536
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi83 – 87Combined sources5
Beta strandi93 – 95Combined sources3
Beta strandi97 – 102Combined sources6
Helixi103 – 105Combined sources3
Helixi107 – 113Combined sources7
Helixi116 – 118Combined sources3
Helixi120 – 126Combined sources7
Beta strandi131 – 141Combined sources11
Helixi142 – 148Combined sources7
Turni151 – 153Combined sources3
Beta strandi154 – 158Combined sources5
Beta strandi161 – 164Combined sources4
Beta strandi168 – 170Combined sources3
Beta strandi174 – 178Combined sources5
Beta strandi183 – 188Combined sources6
Turni189 – 192Combined sources4
Beta strandi195 – 212Combined sources18
Turni213 – 216Combined sources4
Beta strandi231 – 233Combined sources3
Beta strandi238 – 243Combined sources6
Beta strandi245 – 248Combined sources4
Beta strandi257 – 262Combined sources6
Helixi266 – 272Combined sources7
Beta strandi278 – 283Combined sources6
Beta strandi285 – 288Combined sources4
Beta strandi290 – 297Combined sources8
Beta strandi302 – 305Combined sources4
Beta strandi307 – 310Combined sources4
Beta strandi312 – 321Combined sources10
Beta strandi326 – 329Combined sources4
Beta strandi331 – 333Combined sources3
Beta strandi336 – 338Combined sources3
Beta strandi340 – 346Combined sources7
Beta strandi351 – 354Combined sources4
Beta strandi356 – 359Combined sources4
Beta strandi364 – 370Combined sources7
Beta strandi375 – 378Combined sources4
Beta strandi380 – 382Combined sources3
Beta strandi388 – 393Combined sources6
Beta strandi398 – 401Combined sources4
Beta strandi403 – 405Combined sources3
Beta strandi411 – 416Combined sources6
Beta strandi419 – 424Combined sources6
Beta strandi426 – 429Combined sources4
Beta strandi431 – 438Combined sources8
Turni449 – 451Combined sources3
Beta strandi459 – 469Combined sources11
Beta strandi471 – 477Combined sources7
Beta strandi481 – 487Combined sources7
Beta strandi489 – 491Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NK6X-ray2.10A46-536[»]
4NK8X-ray2.29A46-536[»]
4OZYX-ray2.90A69-491[»]
4OZZX-ray2.90A69-492[»]
ProteinModelPortaliQ887Q3.
SMRiQ887Q3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati298 – 320PbH1 1Add BLAST23
Repeati322 – 345PbH1 2Add BLAST24
Repeati347 – 369PbH1 3Add BLAST23
Repeati371 – 393PbH1 4Add BLAST23
Repeati394 – 416PbH1 5Add BLAST23

Sequence similaritiesi

Belongs to the D-mannuronate C5-epimerase family.Curated
Contains 5 PbH1 repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4108C0K. Bacteria.
ENOG41101XF. LUCA.
HOGENOMiHOG000270136.
KOiK01795.
OMAiHDRSHGL.
OrthoDBiPOG091H0SSS.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR022441. Para_beta_helix_rpt-2.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SMARTiSM00722. CASH. 1 hit.
SM00710. PbH1. 5 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.

Q887Q3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSHASNGRS RNWPHALLES ALLTSALLMA SSVALANAPA VPEAPKALVK
60 70 80 90 100
ELHQAKTYTI TSPPTGPLEM AKPVLPDLSG YTTEAALKKI ARNKPGKITV
110 120 130 140 150
ARMMEETGLK EFIGGDNKMA EWVVRQKGIP QAIMISDGYV NLQDLVKKVP
160 170 180 190 200
KQFLSEVSPG VYVARLPILV KETGIFEIDS KTKELRLSQE KGSFIVSEGK
210 220 230 240 250
MLITNTSVNA WSETRNGLAA YRTPDEFRPF VLTWGGSQTW IAKTKMASMG
260 270 280 290 300
YNQSKSYGVS ISQYTPNTAK VLKRGEPTGW IIDSEFADMW YGFYCYETRD
310 320 330 340 350
FVVKGNTYRD NIVYGIDPHD RSHGLIIAEN DVYGTKKKHG IIISREVDNS
360 370 380 390 400
FIFRNKSHNN KLSGVVLDRN SVGNIVAYNE IYQNHTDGIT LYESGNNLLW
410 420 430 440 450
GNRVIANRRH GIRVRNSVNI KLYENVAMAN GLMGVYGHIK DLNDTDRDIE
460 470 480 490 500
LDPFDAQVSL IMVGGELSSN GSGPLSIDSP LSVELYRVSM LMPTKEVGIS
510 520 530
LNGILGERQD EILDLLVRQK KAVLIDPVES QTELRE
Length:536
Mass (Da):59,486
Last modified:June 1, 2003 - v1
Checksum:iB17F41A67C6AA854
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016853 Genomic DNA. Translation: AAO54763.1.
RefSeqiNP_791068.1. NC_004578.1.
WP_011103483.1. NC_004578.1.

Genome annotation databases

EnsemblBacteriaiAAO54763; AAO54763; PSPTO_1238.
GeneIDi1182874.
KEGGipst:PSPTO_1238.
PATRICi19993716. VBIPseSyr93040_1259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016853 Genomic DNA. Translation: AAO54763.1.
RefSeqiNP_791068.1. NC_004578.1.
WP_011103483.1. NC_004578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NK6X-ray2.10A46-536[»]
4NK8X-ray2.29A46-536[»]
4OZYX-ray2.90A69-491[»]
4OZZX-ray2.90A69-492[»]
ProteinModelPortaliQ887Q3.
SMRiQ887Q3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi223283.PSPTO_1238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO54763; AAO54763; PSPTO_1238.
GeneIDi1182874.
KEGGipst:PSPTO_1238.
PATRICi19993716. VBIPseSyr93040_1259.

Phylogenomic databases

eggNOGiENOG4108C0K. Bacteria.
ENOG41101XF. LUCA.
HOGENOMiHOG000270136.
KOiK01795.
OMAiHDRSHGL.
OrthoDBiPOG091H0SSS.

Enzyme and pathway databases

UniPathwayiUPA00286.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR022441. Para_beta_helix_rpt-2.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SMARTiSM00722. CASH. 1 hit.
SM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR03804. para_beta_helix. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiALGG_PSESM
AccessioniPrimary (citable) accession number: Q887Q3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 87 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

3D-structure, Complete proteome, 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

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.