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Protein

Poly(beta-D-mannuronate) C5 epimerase 4

Gene

algE4

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 3 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)DescriptionActionsGraphical viewLength
ChainiPRO_00002195581 – 553Poly(beta-D-mannuronate) C5 epimerase 4Add BLAST553

Expressioni

Developmental stagei

Produced in encysting cells.

Interactioni

Protein-protein interaction databases

STRINGi322710.Avin_51200.

Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 8Combined sources4
Beta strandi13 – 17Combined sources5
Helixi19 – 31Combined sources13
Beta strandi34 – 39Combined sources6
Beta strandi41 – 46Combined sources6
Helixi52 – 54Combined sources3
Beta strandi56 – 58Combined sources3
Beta strandi63 – 70Combined sources8
Beta strandi73 – 77Combined sources5
Beta strandi85 – 90Combined sources6
Beta strandi98 – 108Combined sources11
Helixi111 – 113Combined sources3
Beta strandi118 – 123Combined sources6
Beta strandi133 – 144Combined sources12
Beta strandi150 – 153Combined sources4
Beta strandi155 – 164Combined sources10
Beta strandi166 – 169Combined sources4
Beta strandi174 – 187Combined sources14
Beta strandi189 – 192Combined sources4
Beta strandi197 – 201Combined sources5
Beta strandi205 – 211Combined sources7
Beta strandi213 – 216Combined sources4
Beta strandi221 – 225Combined sources5
Beta strandi228 – 230Combined sources3
Beta strandi235 – 241Combined sources7
Beta strandi243 – 246Combined sources4
Beta strandi251 – 264Combined sources14
Beta strandi266 – 269Combined sources4
Beta strandi274 – 287Combined sources14
Beta strandi289 – 292Combined sources4
Beta strandi295 – 298Combined sources4
Beta strandi301 – 305Combined sources5
Beta strandi312 – 314Combined sources3
Beta strandi324 – 327Combined sources4
Beta strandi329 – 331Combined sources3
Beta strandi338 – 342Combined sources5
Beta strandi344 – 346Combined sources3
Beta strandi351 – 354Combined sources4
Beta strandi356 – 365Combined sources10
Beta strandi372 – 374Combined sources3
Beta strandi393 – 398Combined sources6
Beta strandi401 – 403Combined sources3
Beta strandi406 – 408Combined sources3
Beta strandi411 – 417Combined sources7
Beta strandi419 – 421Combined sources3
Beta strandi424 – 426Combined sources3
Beta strandi428 – 434Combined sources7
Beta strandi437 – 439Combined sources3
Beta strandi442 – 444Combined sources3
Beta strandi457 – 461Combined sources5
Turni463 – 465Combined sources3
Beta strandi467 – 469Combined sources3
Beta strandi471 – 474Combined sources4
Beta strandi479 – 482Combined sources4
Beta strandi486 – 490Combined sources5
Beta strandi494 – 502Combined sources9
Turni506 – 508Combined sources3
Beta strandi514 – 519Combined sources6
Turni525 – 527Combined sources3
Beta strandi542 – 544Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ44493.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati133 – 155PbH1 1Add BLAST23
Repeati157 – 179PbH1 2Add BLAST23
Repeati180 – 202PbH1 3Add BLAST23
Repeati204 – 226PbH1 4Add BLAST23
Repeati234 – 256PbH1 5Add BLAST23
Repeati257 – 279PbH1 6Add BLAST23
Repeati280 – 301PbH1 7Add BLAST22
Repeati320 – 342PbH1 8Add BLAST23
Repeati403 – 420Hemolysin-type calcium-binding 1Add BLAST18
Repeati421 – 438Hemolysin-type calcium-binding 2Add BLAST18

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AGMNMR-A387-553[»]
2PYGX-ray2.10A/B1-377[»]
2PYHX-ray2.70A/B1-377[»]
ProteinModelPortaliQ44493.
SMRiQ44493.
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...

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: November 2, 2016
This is version 82 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.