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Protein

Poly(beta-D-mannuronate) C5 epimerase 4

Gene

algE4

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), but introduces almost exclusively MG blocks, producing a polymer with non-gel-forming capacity.

Cofactori

Enzyme regulationi

Inhibited by zinc.

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

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14389.
UniPathwayiUPA00286.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(beta-D-mannuronate) C5 epimerase 4 (EC:5.1.3.-)
Alternative name(s):
Mannuronan epimerase 4
Gene namesi
Name:algE4
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Poly(beta-D-mannuronate) C5 epimerase 4PRO_0000219558Add
BLAST

Expressioni

Developmental stagei

Produced in encysting cells.

Interactioni

Protein-protein interaction databases

STRINGi322710.Avin_51200.

Structurei

Secondary structure

1
553
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Beta strandi13 – 175Combined sources
Helixi19 – 3113Combined sources
Beta strandi34 – 396Combined sources
Beta strandi41 – 466Combined sources
Helixi52 – 543Combined sources
Beta strandi56 – 583Combined sources
Beta strandi63 – 708Combined sources
Beta strandi73 – 775Combined sources
Beta strandi85 – 906Combined sources
Beta strandi98 – 10811Combined sources
Helixi111 – 1133Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi133 – 14412Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi155 – 16410Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi174 – 18714Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi205 – 2117Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi221 – 2255Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi235 – 2417Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi251 – 26414Combined sources
Beta strandi266 – 2694Combined sources
Beta strandi274 – 28714Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi295 – 2984Combined sources
Beta strandi301 – 3055Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi324 – 3274Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi338 – 3425Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi351 – 3544Combined sources
Beta strandi356 – 36510Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi393 – 3986Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi406 – 4083Combined sources
Beta strandi411 – 4177Combined sources
Beta strandi419 – 4213Combined sources
Beta strandi424 – 4263Combined sources
Beta strandi428 – 4347Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi442 – 4443Combined sources
Beta strandi457 – 4615Combined sources
Turni463 – 4653Combined sources
Beta strandi467 – 4693Combined sources
Beta strandi471 – 4744Combined sources
Beta strandi479 – 4824Combined sources
Beta strandi486 – 4905Combined sources
Beta strandi494 – 5029Combined sources
Turni506 – 5083Combined sources
Beta strandi514 – 5196Combined sources
Turni525 – 5273Combined sources
Beta strandi542 – 5443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGMNMR-A387-553[»]
2PYGX-ray2.10A/B1-377[»]
2PYHX-ray2.70A/B1-377[»]
ProteinModelPortaliQ44493.
SMRiQ44493. Positions 1-377, 387-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ44493.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati133 – 15523PbH1 1Add
BLAST
Repeati157 – 17923PbH1 2Add
BLAST
Repeati180 – 20223PbH1 3Add
BLAST
Repeati204 – 22623PbH1 4Add
BLAST
Repeati234 – 25623PbH1 5Add
BLAST
Repeati257 – 27923PbH1 6Add
BLAST
Repeati280 – 30122PbH1 7Add
BLAST
Repeati320 – 34223PbH1 8Add
BLAST
Repeati403 – 42018Hemolysin-type calcium-binding 1Add
BLAST
Repeati421 – 43818Hemolysin-type calcium-binding 2Add
BLAST

Domaini

Composed of one catalytically active A module and one R module.

Sequence similaritiesi

Belongs to the D-mannuronate C5-epimerase family.Curated
Contains 8 PbH1 repeats.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR018511. Hemolysin-typ_Ca-bd_CS.
IPR006626. PbH1.
IPR024535. Pectate_lyase_SF_prot.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF12708. Pectate_lyase_3. 1 hit.
[Graphical view]
SMARTiSM00722. CASH. 2 hits.
SM00710. PbH1. 8 hits.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 1 hit.
SSF51126. SSF51126. 1 hit.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q44493-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYNVKDFGA LGDGVSDDRA SIQAAIDAAY AAGGGTVYLP AGEYRVSAAG
60 70 80 90 100
EPGDGCLMLK DGVYLAGAGM GETVIKLIDG SDQKITGMVR SAYGEETSNF
110 120 130 140 150
GMRDLTLDGN RDNTSGKVDG WFNGYIPGGD GADRDVTIER VEVREMSGYG
160 170 180 190 200
FDPHEQTINL TIRDSVAHDN GLDGFVADYL VDSVFENNVA YANDRHGFNV
210 220 230 240 250
VTSTHDFVMT NNVAYGNGSS GLVVQRGLED LALPSNILID GGAYYDNARE
260 270 280 290 300
GVLLKMTSDI TLQNADIHGN GSSGVRVYGA QDVQILDNQI HDNAQAAAVP
310 320 330 340 350
EVLLQSFDDT AGASGTYYTT LNTRIEGNTI SGSANSTYGI QERNDGTDYS
360 370 380 390 400
SLIDNDIAGV QQPIQLYGPH STVSGEPGAT PQQPSTGSDG EPLVGGDTDD
410 420 430 440 450
QLQGGSGADR LDGGAGDDIL DGGAGRDRLS GGAGADTFVF SAREDSYRTD
460 470 480 490 500
TAVFNDLILD FEASEDRIDL SALGFSGLGD GYGGTLLLKT NAEGTRTYLK
510 520 530 540 550
SFEADAEGRR FEVALDGDHT GDLSAANVVF AATGTTTELE VLGDSGTQAG

AIV
Length:553
Mass (Da):57,709
Last modified:November 1, 1996 - v1
Checksum:i2806B4AEA3FFF128
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39096 Genomic DNA. Translation: AAA87310.1.
PIRiS77623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39096 Genomic DNA. Translation: AAA87310.1.
PIRiS77623.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGMNMR-A387-553[»]
2PYGX-ray2.10A/B1-377[»]
2PYHX-ray2.70A/B1-377[»]
ProteinModelPortaliQ44493.
SMRiQ44493. Positions 1-377, 387-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_51200.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00286.
BioCyciMetaCyc:MONOMER-14389.

Miscellaneous databases

EvolutionaryTraceiQ44493.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR018511. Hemolysin-typ_Ca-bd_CS.
IPR006626. PbH1.
IPR024535. Pectate_lyase_SF_prot.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF12708. Pectate_lyase_3. 1 hit.
[Graphical view]
SMARTiSM00722. CASH. 2 hits.
SM00710. PbH1. 8 hits.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 1 hit.
SSF51126. SSF51126. 1 hit.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A family of modular type mannuronan C-5-epimerase genes controls alginate structure in Azotobacter vinelandii."
    Ertesvaag H., Hoeidal H.K., Hals I.K., Rian A., Doseth B., Valla S.
    Mol. Microbiol. 16:719-731(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: E.
  2. "The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism."
    Hoeidal H.K., Ertesvaag H., Skjaak-Braek G., Stokke B.T., Valla S.
    J. Biol. Chem. 274:12316-12322(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: E.
  3. "Mannuronan C-5 epimerases and cellular differentiation of Azotobacter vinelandii."
    Hoeidal H.K., Glaerum Svanem B.I., Gimmestad M., Valla S.
    Environ. Microbiol. 2:27-38(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPRESSION.
    Strain: E.
  4. "Mannuronan C-5-epimerases and their application for in vitro and in vivo design of new alginates useful in biotechnology."
    Ertesvaag H., Hoeidal H.K., Schjerven H., Glaerum Svanem B.I., Valla S.
    Metab. Eng. 1:262-269(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiALGE4_AZOVI
AccessioniPrimary (citable) accession number: Q44493
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Each enzyme of this family of C5 epimerases introduces its own characteristic sequence distribution of G-blocks in their substrates, explaining the extensive sequence variability of alginates. These alginates of varying composition have different physical properties and are necessary at different stages of the bacterium life cycle.

Keywords - Technical termi

3D-structure

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.