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Database: UniProt
Entry: ALGE5_AZOVI
LinkDB: ALGE5_AZOVI
Original site: ALGE5_AZOVI 
ID   ALGE5_AZOVI             Reviewed;         997 AA.
AC   Q44492;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-MAY-2023, entry version 105.
DE   RecName: Full=Mannuronan C5-epimerase AlgE5 {ECO:0000305};
DE            EC=5.1.3.37 {ECO:0000250|UniProtKB:Q44494};
DE   AltName: Full=Poly(beta-D-mannuronate) C5 epimerase 5;
GN   Name=algE5 {ECO:0000303|PubMed:7476166};
OS   Azotobacter vinelandii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E;
RX   PubMed=7476166; DOI=10.1111/j.1365-2958.1995.tb02433.x;
RA   Ertesvaag H., Hoeidal H.K., Hals I.K., Rian A., Doseth B., Valla S.;
RT   "A family of modular type mannuronan C-5-epimerase genes controls alginate
RT   structure in Azotobacter vinelandii.";
RL   Mol. Microbiol. 16:719-731(1995).
RN   [2]
RP   EXPRESSION.
RC   STRAIN=E;
RX   PubMed=11243259; DOI=10.1046/j.1462-2920.2000.00074.x;
RA   Hoeidal H.K., Glaerum Svanem B.I., Gimmestad M., Valla S.;
RT   "Mannuronan C-5 epimerases and cellular differentiation of Azotobacter
RT   vinelandii.";
RL   Environ. Microbiol. 2:27-38(2000).
RN   [3]
RP   REVIEW.
RX   PubMed=10937941; DOI=10.1006/mben.1999.0130;
RA   Ertesvaag H., Hoeidal H.K., Schjerven H., Glaerum Svanem B.I., Valla S.;
RT   "Mannuronan C-5-epimerases and their application for in vitro and in vivo
RT   design of new alginates useful in biotechnology.";
RL   Metab. Eng. 1:262-269(1999).
CC   -!- FUNCTION: Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid
CC       (G), producing a polymer with gel-forming capacity, required for the
CC       formation of the cyst coat. {ECO:0000250|UniProtKB:Q44494}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-beta-D-mannuronosyl](n) = [alginate](n);
CC         Xref=Rhea:RHEA:45572, Rhea:RHEA-COMP:11264, Rhea:RHEA-COMP:11270,
CC         ChEBI:CHEBI:58187, ChEBI:CHEBI:85311; EC=5.1.3.37;
CC         Evidence={ECO:0000250|UniProtKB:Q44494};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q44494};
CC   -!- ACTIVITY REGULATION: Inhibited by zinc. {ECO:0000250|UniProtKB:Q44494}.
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC       {ECO:0000250|UniProtKB:Q44494}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Probably exported via the
CC       hemolysin-type secretion pathway.
CC   -!- DEVELOPMENTAL STAGE: Produced during vegetative growth and in encysting
CC       cells.
CC   -!- DOMAIN: Composed of one catalytically active A module and four R
CC       modules.
CC   -!- MISCELLANEOUS: Each enzyme of this family of C5 epimerases introduces
CC       its own characteristic sequence distribution of G-blocks in their
CC       substrates, explaining the extensive sequence variability of alginates.
CC       These alginates of varying composition have different physical
CC       properties and are necessary at different stages of the bacterium life
CC       cycle.
CC   -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; L39013; AAA87309.1; -; Genomic_DNA.
DR   PIR; I39739; I39739.
DR   AlphaFoldDB; Q44492; -.
DR   SMR; Q44492; -.
DR   BRENDA; 5.1.3.37; 49.
DR   UniPathway; UPA00286; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 3.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR   PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR   Pfam; PF13229; Beta_helix; 1.
DR   Pfam; PF00353; HemolysinCabind; 4.
DR   Pfam; PF12708; Pectate_lyase_3; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00722; CASH; 2.
DR   SMART; SM00710; PbH1; 7.
DR   SUPFAM; SSF51120; beta-Roll; 4.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
PE   2: Evidence at transcript level;
KW   Alginate biosynthesis; Calcium; Isomerase; Repeat; Secreted.
FT   CHAIN           1..997
FT                   /note="Mannuronan C5-epimerase AlgE5"
FT                   /id="PRO_0000219559"
FT   REPEAT          133..155
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          157..179
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          180..202
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          204..226
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          257..279
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          280..315
FT                   /note="PbH1 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          320..359
FT                   /note="PbH1 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          388..403
FT                   /note="Hemolysin-type calcium-binding 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          406..422
FT                   /note="Hemolysin-type calcium-binding 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          424..439
FT                   /note="Hemolysin-type calcium-binding 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          557..573
FT                   /note="Hemolysin-type calcium-binding 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          574..590
FT                   /note="Hemolysin-type calcium-binding 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          695..709
FT                   /note="Hemolysin-type calcium-binding 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          712..729
FT                   /note="Hemolysin-type calcium-binding 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          828..839
FT                   /note="Hemolysin-type calcium-binding 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          846..862
FT                   /note="Hemolysin-type calcium-binding 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          864..880
FT                   /note="Hemolysin-type calcium-binding 10"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   997 AA;  103724 MW;  76C3E05504DCFB99 CRC64;
     MDYNVKDFGA LGDGVSDDTA AIQAAIDAAY AAGGGTVYLP AGEYRVSGGE EPSDGCLTIK
     SNVYIVGAGM GETVIKLVDG WDQDVTGIVR SAYGEETSNF GMSDLTLDGN RDNTSGKVDG
     WFNGYIPGED GADRDVTLER VEIREMSGYG FDPHEQTINL TIRDSVAHDN GLDGFVADFQ
     IGGVFENNVS YNNDRHGFNI VTSTNDFVLS NNVAYGNGGA GLVIQRGSYD VAHPYGILID
     GGAYYDNGLE GVQIKMAHDV TLQNAEIYGN GLYGVRVYGA EDVQILDNYI HDNSQSGSYA
     EILLQSYDDT AGVSGNFYTT TGTWIEGNTI VGSANSTYGI QERADGTDYS SLYANSVSNV
     QSGSVRLYGT NSVVSDLPGT GQQATLEGTT GNDTLTGSEA HETLLGLDGN DRLNGGAGND
     ILDGGAGRDN LTGGAGADLF RVSARTDSYR TDSASFNDLI TDFDPAQDRI DLSALGFTGL
     GDGYNGTLAV VLNSAGTRTY LKSYEADAEG RRFEIALDGN FAGLLDDGNL IFERPVIEGD
     AGNNALLGTS AAETLLGHAG NDTLDGAGGD DILVGGAGRD TLTGGAGADL FRFDALSDSQ
     RNYTTGDNQG DRIVDFSVGE DKLDVSALGF TGLGDGYNGT LAVVVNSAGD RTYVKSYETD
     ADGYRFEFSL EGNYQDLGSE SFVFATPSGQ QLLEGSAGND SLQGTAADEI VHGGAGRDTL
     SGGAGADVFR FSELTDSYRT ASTSFADLIT DFDLADDRID LSGLGFSGLG DGYDGTLAVV
     VNSTGTRTYL KSYEANAAGE RFEIALDGDL SAFTGANLIL DERVVLEGSD GNDTLDGGSA
     AEELLGGAGN DSLDGGAGND ILDGGAGRDT LSGGSGSDIF RYDDALDSFR NYGTGVTGTD
     TITDFTPGED LIDLSALGYT GLGDGYNGTL AVVLNGDGTR TYLKDRESDA EGNQFEIALD
     GDLVDRLDAG DFIFAEAAAT TAIEVVGGTP TEEQLVA
//
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