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Protein

Mannuronan C5-epimerase AlgE4

Gene

algE4

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: -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.1 Publication

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.

Catalytic activityi

(Mannuronan)-beta-D-mannuronate = (alginate)-alpha-L-guluronate.1 Publication

Cofactori

Ca2+1 Publication

Enzyme regulationi

Inhibited by zinc.1 Publication

Kineticsi

kcat is 14 sec(-1).1 Publication
    1. Vmax=14.8 µmol/min/mg enzyme1 Publication

    pH dependencei

    Optimum pH is 6.5-7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius.1 Publication

    Pathwayi: alginate biosynthesis

    This protein is involved in the pathway alginate biosynthesis, which is part of Glycan biosynthesis.Curated
    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

    Keywordsi

    Molecular functionIsomerase
    Biological processAlginate biosynthesis
    LigandCalcium

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14389
    UniPathwayiUPA00286

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannuronan C5-epimerase AlgE4Curated (EC:5.1.3.371 Publication)
    Alternative name(s):
    Poly(beta-D-mannuronate) C5 epimerase 4
    Gene namesi
    Name:algE41 Publication
    OrganismiAzotobacter vinelandii
    Taxonomic identifieri354 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002195581 – 553Mannuronan C5-epimerase AlgE4Add BLAST553

    Proteomic databases

    PRIDEiQ44493

    Expressioni

    Developmental stagei

    Produced in encysting cells.

    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 1Sequence analysisAdd BLAST23
    Repeati157 – 179PbH1 2Sequence analysisAdd BLAST23
    Repeati180 – 202PbH1 3Sequence analysisAdd BLAST23
    Repeati204 – 226PbH1 4Sequence analysisAdd BLAST23
    Repeati234 – 256PbH1 5Sequence analysisAdd BLAST23
    Repeati257 – 279PbH1 6Sequence analysisAdd BLAST23
    Repeati280 – 301PbH1 7Sequence analysisAdd BLAST22
    Repeati320 – 342PbH1 8Sequence analysisAdd 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

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di2.150.10.10, 1 hit
    2.160.20.10, 1 hit
    InterProiView protein in InterPro
    IPR006633 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
    PfamiView protein in Pfam
    PF12708 Pectate_lyase_3, 1 hit
    SMARTiView protein in SMART
    SM00722 CASH, 2 hits
    SM00710 PbH1, 8 hits
    SUPFAMiSSF51120 SSF51120, 1 hit
    SSF51126 SSF51126, 1 hit
    PROSITEiView protein in PROSITE
    PS00330 HEMOLYSIN_CALCIUM, 3 hits

    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

    Similar proteinsi

    Entry informationi

    Entry nameiALGE4_AZOVI
    AccessioniPrimary (citable) accession number: Q44493
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2003
    Last sequence update: November 1, 1996
    Last modified: May 23, 2018
    This is version 87 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

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