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Protein

Poly(beta-D-mannuronate) C5 epimerase 1

Gene

algE1

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

Functioni

Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), producing a polymer with gel-forming capacity, required for the formation of the cyst coat.

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

UniPathwayiUPA00286.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(beta-D-mannuronate) C5 epimerase 1 (EC:5.1.3.-)
Alternative name(s):
Mannuronan epimerase 1
Gene namesi
Name:algE1
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_00002195551 – 1403Poly(beta-D-mannuronate) C5 epimerase 1Add BLAST1403

Expressioni

Developmental stagei

Produced during vegetative growth and in encysting cells.

Interactioni

Protein-protein interaction databases

STRINGi322710.Avin_51190.

Structurei

3D structure databases

ProteinModelPortaliQ44494.
ModBaseiSearch...
MobiDBiSearch...

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
Repeati257 – 279PbH1 5Add BLAST23
Repeati280 – 302PbH1 6Add BLAST23
Repeati320 – 359PbH1 7Add BLAST40
Repeati387 – 404Hemolysin-type calcium-binding 1Add BLAST18
Repeati405 – 422Hemolysin-type calcium-binding 2Add BLAST18
Repeati423 – 440Hemolysin-type calcium-binding 3Add BLAST18
Repeati538 – 555Hemolysin-type calcium-binding 4Add BLAST18
Repeati556 – 573Hemolysin-type calcium-binding 5Add BLAST18
Repeati574 – 591Hemolysin-type calcium-binding 6Add BLAST18
Repeati697 – 714Hemolysin-type calcium-binding 7Add BLAST18
Repeati715 – 732Hemolysin-type calcium-binding 8Add BLAST18
Repeati733 – 750Hemolysin-type calcium-binding 9Add BLAST18
Repeati977 – 999PbH1 8Add BLAST23
Repeati1001 – 1023PbH1 9Add BLAST23
Repeati1024 – 1046PbH1 10Add BLAST23
Repeati1048 – 1070PbH1 11Add BLAST23
Repeati1101 – 1123PbH1 12Add BLAST23
Repeati1124 – 1146PbH1 13Add BLAST23
Repeati1163 – 1185PbH1 14Add BLAST23
Repeati1190 – 1212PbH1 15Add BLAST23
Repeati1226 – 1243Hemolysin-type calcium-binding 10Add BLAST18
Repeati1244 – 1261Hemolysin-type calcium-binding 11Add BLAST18
Repeati1262 – 1279Hemolysin-type calcium-binding 12Add BLAST18

Domaini

Composed of two catalytically active A modules and four R modules. The N-terminal A domain introduces a mixture of MG-blocks and G- blocks, whereas the C-terminal A domain only generates MG-blocks.2 Publications

Sequence similaritiesi

Belongs to the D-mannuronate C5-epimerase family.Curated
Contains 15 PbH1 repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105DDI. Bacteria.
COG2931. LUCA.

Family and domain databases

Gene3Di2.150.10.10. 4 hits.
2.160.20.10. 2 hits.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR006626. PbH1.
IPR024535. Pectate_lyase_SF_prot.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF00353. HemolysinCabind. 11 hits.
PF12708. Pectate_lyase_3. 2 hits.
[Graphical view]
SMARTiSM00722. CASH. 4 hits.
SM00710. PbH1. 15 hits.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 4 hits.
SSF51126. SSF51126. 2 hits.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q44494-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYNVKDFGA LGDGVSDDTA AIQAAIDAAH AAGGGTVYLP AGEYRVSGGE
60 70 80 90 100
EPSDGCLTIK SNVHIVGAGM GETVIKMVDG WTQNVTGMVR SAYGEETSNF
110 120 130 140 150
GMSDLTLDGN RDNLSAKVDG WFNGYIPGQD GADRDVTLER VEIREMSGYG
160 170 180 190 200
FDPHEQTINL TIRDSVAHDN SLDGFVADYQ VGGVFENNVS YNNDRHGFNI
210 220 230 240 250
VTSTNDFVLS NNVAYGNGGA GLVVQRGSYD LPHPYDILID GGAYYDNALE
260 270 280 290 300
GVQLKMAHDV TLQNAEIYGN GLYGVRVYGA QDVQILDNQI HDNSQNGAYA
310 320 330 340 350
EVLLQSYDDT AGVSGNFYVT TGTWLEGNVI SGSANSTYGI QERADGTDYS
360 370 380 390 400
SLYANSIDGV QTGAVRLYGA NSTVSSQSGS GQQATLEGSA GNDALSGTEA
410 420 430 440 450
HETLLGQAGD DRLNGDAGND ILDGGAGRDN LTGGAGADTF RFSARTDSYR
460 470 480 490 500
TDSASFNDLI TDFDADEDSI DLSALGFTGL GDGYNGTLLL KTNAEGTRTY
510 520 530 540 550
LKSYEADAQG RRFEIALDGN FTGLFNDNNL LFDAAPATGT EGSDNLLGTD
560 570 580 590 600
AGETLLGYGG NDTLNGGAGD DILVGGAGRD SLTGGAGADV FRFDALSDSQ
610 620 630 640 650
RNYTTGDNQA DRILDFDPTL DRIDVSALGF TGLGNGRNGT LAVVLNSAGD
660 670 680 690 700
RTDLKSYDTD ANGYSFELSL AGNYQGQLSA EQFVFATSQG GQMTIIEGTD
710 720 730 740 750
GNDTLQGTEA NERLLGLDGR DNLNGGAGDD ILDGGAGRDT LTGGTGADTF
760 770 780 790 800
LFSTRTDSYR TDSASFNDLI TDFDPTQDRI DLSGLGFSGF GNGYDGTLLL
810 820 830 840 850
QVNAAGTRTY LKSFEADANG QRFEIALDGD FSGQLDSGNV IFEPAVFNAK
860 870 880 890 900
DFGALGDGAS DDRPAIQAAI DAAYAAGGGT VYLPAGEYRV SPTGEPGDGC
910 920 930 940 950
LMLKDGVYLA GDGIGETVIK LIDGSDQKIT GMVRSAYGEE TSNFGMSDLT
960 970 980 990 1000
LDGNRDNTSG KVDGWFNGYI PGQDGADRNV TIERVEIREM SGYGFDPHEQ
1010 1020 1030 1040 1050
TINLTIRDSV AHDNGLDGFV ADYLVDSVFE NNVAYNNDRH GFNIVTSTYD
1060 1070 1080 1090 1100
FVMTNNVAYG NGGAGLTIQR GSEDLAQPTD ILIDGGAYYD NALEGVLFKM
1110 1120 1130 1140 1150
TNNVTLQNAE IYGNGSSGVR LYGTEDVQIL DNQIHDNSQN GTYPEVLLQA
1160 1170 1180 1190 1200
FDDSQVTGEL YETLNTRIEG NLIDASDNAN YAVRERDDGS DYTTLVDNDI
1210 1220 1230 1240 1250
SGGQVASVQL SGAHSSLSGG TVEVPQGTDG NDVLVGSDAN DQLYGGAGDD
1260 1270 1280 1290 1300
RLDGGAGDDL LDGGAGRDDL TGGTGADTFV FAARTDSYRT DAGVFNDLIL
1310 1320 1330 1340 1350
DFDASEDRID LSALGFSGFG DGYNGTLLVQ LSSAGTRTYL KSYEEDLEGR
1360 1370 1380 1390 1400
RFEVALDGDH TGDLSAANVV FADDGSAAVA SSDPAATQLE VVGSSGTQTD

QLA
Length:1,403
Mass (Da):147,169
Last modified:November 1, 1996 - v1
Checksum:i4E843AB0A366A95C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39096 Genomic DNA. Translation: AAA87311.1.
PIRiS77624.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39096 Genomic DNA. Translation: AAA87311.1.
PIRiS77624.

3D structure databases

ProteinModelPortaliQ44494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_51190.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DDI. Bacteria.
COG2931. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00286.

Family and domain databases

Gene3Di2.150.10.10. 4 hits.
2.160.20.10. 2 hits.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR006626. PbH1.
IPR024535. Pectate_lyase_SF_prot.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF00353. HemolysinCabind. 11 hits.
PF12708. Pectate_lyase_3. 2 hits.
[Graphical view]
SMARTiSM00722. CASH. 4 hits.
SM00710. PbH1. 15 hits.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 4 hits.
SSF51126. SSF51126. 2 hits.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 9 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALGE1_AZOVI
AccessioniPrimary (citable) accession number: Q44494
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 85 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.

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.