ALGE2_AZOVI
ID ALGE2_AZOVI Reviewed; 997 AA.
AC Q44495;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Mannuronan C5-epimerase AlgE2 {ECO:0000305};
DE EC=5.1.3.37 {ECO:0000269|PubMed:8188585};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase 2;
GN Name=algE2 {ECO:0000303|PubMed:7476166};
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=E;
RX PubMed=8188585; DOI=10.1128/jb.176.10.2846-2853.1994;
RA Ertesvaag H., Doseth B., Larsen B., Skjaak-Braek G., Valla S.;
RT "Cloning and expression of an Azotobacter vinelandii mannuronan C-5-
RT epimerase gene.";
RL J. Bacteriol. 176:2846-2853(1994).
RN [2]
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 [3]
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 [4]
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:0000269|PubMed:8188585}.
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:0000269|PubMed:8188585};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- ACTIVITY REGULATION: Inhibited by zinc.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Probably exported via the
CC hemolysin-type secretion pathway.
CC -!- DEVELOPMENTAL STAGE: Produced mainly in encysting 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; L39096; AAA87312.1; -; Genomic_DNA.
DR PIR; S77625; S77625.
DR AlphaFoldDB; Q44495; -.
DR SMR; Q44495; -.
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; -; 3.
DR Gene3D; 2.160.20.10; -; 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 Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF00353; HemolysinCabind; 4.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SMART; SM00722; CASH; 2.
DR SMART; SM00710; PbH1; 7.
DR SUPFAM; SSF51120; SSF51120; 4.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
PE 1: Evidence at protein level;
KW Alginate biosynthesis; Calcium; Direct protein sequencing; Isomerase;
KW Repeat; Secreted.
FT CHAIN 1..997
FT /note="Mannuronan C5-epimerase AlgE2"
FT /id="PRO_0000219556"
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..591
FT /note="Hemolysin-type calcium-binding 5"
FT /evidence="ECO:0000255"
FT REPEAT 696..711
FT /note="Hemolysin-type calcium-binding 6"
FT /evidence="ECO:0000255"
FT REPEAT 713..730
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; 103084 MW; B3D3C1E57ADAC404 CRC64;
MDYNVKDFGA LGDGVSDDTA AIQAAIDAAY AAGGGTVYLP AGEYRVSGGE EPSDGCLTIK
SNVHIVGAGM GETVIKLVDG WDQDVTGIVR SAYGEETSNF GMSDLTLDGN RDNTSGKVDG
WFNGYIPGED GADRDVTLER VEIREMSGYG FDPHEQTINL TIRDSVAHDN GLDGFVADFQ
IGGVFENNVS YNNDRHGFNI VTSTNDFVLS NNVAYGNGGA GLVVQRGSSD VAHPYDILID
GGAYYDNGLE GVQIKMAHDV TLQNAEIYGN GLYGVRVYGA EDVQILDNYI HDNSQNGSYA
EILLQSYDDT AGVSGNFYTT TGTWIEGNTI VGSANSTYGI QERDDGTDYS SLYANSVSNV
QNGSVRLYGA NSVVSDLPGT GQQATLEGTA GNDTLGGSDA HETLLGLDGN DRLNGGAGND
ILDGGAGRDN LTGGAGADLF RVSARTDSYR TDSASFNDLI TDFDASQDRI DLSALGFTGL
GDGYNGTLLL QVSADGSRTY LKSLEADAEG RRFEIALDGN FAGLLGAGNL LFERTAIEGD
AGDNALLGTS AAETLLGHAG NDTLDGGAGD DILVGGAGRD SLTGGAGADV FRFDALSDSQ
RNYDIGDNQG DRIADFAVGE DKLDVSALGF TGLGDGYNGT LALVLNSAGD RTYVKSYENG
ADGYRFEFSL DGNYLELLGN EDFIFATPSG QQLLEGSAGN DSLQGTAADE VIHGGGGRDT
LAGGAGADVF RFSELTDSYR DSASYADLIT DFDASEDRID LSGLGFSGLG NGYGGTLALQ
VNSAGTRTYL KSFETNAAGE RFEIALDGDL SALGGANLIL DARTVLAGGD GNDTLSGSSA
AEELLGGVGN DSLDGGAGND ILDGGAGRDT LSGGSGSDIF RFGGALDSFR NYASGTNGTD
SITDFTPGED LIDLSVLGYT GLGDGYNGTL AIVLNDAGTK TYLKNRESDA EGNQFEIALE
GNHADQLDAS DFIFATAAAT TGIEVVGGSG TQTDQLA
