ALGE7_AZOVI
ID ALGE7_AZOVI Reviewed; 856 AA.
AC Q9ZFG9;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Alginate lyase 7 {ECO:0000305};
DE EC=4.2.2.3 {ECO:0000269|PubMed:11390391};
DE AltName: Full=Mannuronan C5-epimerase AlgE7 {ECO:0000305};
DE EC=5.1.3.37 {ECO:0000269|PubMed:9864314, ECO:0000305|PubMed:11390391};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase 7;
DE AltName: Full=Poly(beta-D-mannuronate) lyase 7;
DE AltName: Full=Poly(mana) alginate lyase 7;
GN Name=algE7 {ECO:0000303|PubMed:9864314};
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=E;
RX PubMed=9864314; DOI=10.1128/jb.181.1.68-77.1999;
RA Glaerum Svanem B.I., Skjaak-Braek G., Ertesvaag H., Valla S.;
RT "Cloning and expression of three new Azotobacter vinelandii genes closely
RT related to a previously described gene family encoding mannuronan C-5-
RT epimerases.";
RL J. Bacteriol. 181:68-77(1999).
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 FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-152, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=E;
RX PubMed=11390391; DOI=10.1074/jbc.m102562200;
RA Glaerum Svanem B.I., Strand W.I., Ertesvaag H., Skjaak-Braek G.,
RA Hartmann M., Barbeyron T., Valla S.;
RT "The catalytic activities of the bifunctional Azotobacter vinelandii
RT mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from
RT the same active site in the enzyme.";
RL J. Biol. Chem. 276:31542-31550(2001).
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). Has both epimerase and lyase activities. Contributes to abortive
CC encystment by degrading the coat from inside the cyst. Important for
CC cyst germination. {ECO:0000269|PubMed:11390391,
CC ECO:0000269|PubMed:9864314}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of alginate to give oligosaccharides with
CC 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing
CC ends and beta-D-mannuronate at their reducing end.; EC=4.2.2.3;
CC Evidence={ECO:0000269|PubMed:11390391};
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:9864314, ECO:0000305|PubMed:11390391};
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 germinating cells.
CC -!- DOMAIN: Composed of one catalytically active A module and three 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; AF099800; AAD04921.1; -; Genomic_DNA.
DR RefSeq; WP_012703560.1; NZ_FPKM01000015.1.
DR AlphaFoldDB; Q9ZFG9; -.
DR SMR; Q9ZFG9; -.
DR OMA; ISVENNH; -.
DR BRENDA; 4.2.2.3; 49.
DR BRENDA; 5.1.3.37; 49.
DR UniPathway; UPA00286; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0045135; F:poly(beta-D-mannuronate) lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.150.10.10; -; 2.
DR Gene3D; 2.160.20.10; -; 1.
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; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00353; HemolysinCabind; 4.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR SMART; SM00722; CASH; 2.
DR SMART; SM00710; PbH1; 8.
DR SUPFAM; SSF51120; SSF51120; 3.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
PE 1: Evidence at protein level;
KW Alginate biosynthesis; Calcium; Isomerase; Lyase; Repeat; Secreted.
FT CHAIN 1..856
FT /note="Alginate lyase 7"
FT /id="PRO_0000219561"
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 234..256
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 257..279
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT REPEAT 280..304
FT /note="PbH1 7"
FT /evidence="ECO:0000255"
FT REPEAT 320..342
FT /note="PbH1 8"
FT /evidence="ECO:0000255"
FT REPEAT 387..402
FT /note="Hemolysin-type calcium-binding 1"
FT /evidence="ECO:0000255"
FT REPEAT 404..421
FT /note="Hemolysin-type calcium-binding 2"
FT /evidence="ECO:0000255"
FT REPEAT 422..439
FT /note="Hemolysin-type calcium-binding 3"
FT /evidence="ECO:0000255"
FT REPEAT 538..549
FT /note="Hemolysin-type calcium-binding 4"
FT /evidence="ECO:0000255"
FT REPEAT 554..563
FT /note="Hemolysin-type calcium-binding 5"
FT /evidence="ECO:0000255"
FT REPEAT 565..581
FT /note="Hemolysin-type calcium-binding 6"
FT /evidence="ECO:0000255"
FT REPEAT 582..599
FT /note="Hemolysin-type calcium-binding 7"
FT /evidence="ECO:0000255"
FT REPEAT 715..731
FT /note="Hemolysin-type calcium-binding 8"
FT /evidence="ECO:0000255"
FT REPEAT 733..749
FT /note="Hemolysin-type calcium-binding 9"
FT /evidence="ECO:0000255"
FT MUTAGEN 152
FT /note="D->G: Loss of both epimerase and lyase functions."
FT /evidence="ECO:0000269|PubMed:11390391"
SQ SEQUENCE 856 AA; 90364 MW; 626DDCA4681E8807 CRC64;
MEYNVKDFGA KGDGKTDDTD AIQAAIDAAH KAGGGTVYLP SGEYRVSGGD EASDGALIIK
SNVYIVGAGM GETVIKLVDG WDEKLTGIIR SANGEKTHDY GISDLTIDGN QDNTEGEVDG
FYTGYIPGKN GADYNVTVER VEIREVSRYA FDPHEQTINL TIRDSVAHDN GKDGFVADFQ
IGAVFENNVS YNNGRHGFNI VTSSHDIVFT NNVAYGNGAN GLVVQRGSED RDFVYNVEIE
GGSFHDNGQE GVLIKMSTDV TLQGAEIYGN GYAGVRVQGV EDVRILDNYI HDNAQSKANA
EVIVESYDDR DGPSDDYYET QNVTVKGNTI VGSANSTYGI QERADGTDYT SIGNNSVSGT
QRGIVQLSGT NSTFSGRSGD AYQFIDGSTG NDLLTGTPIA DLIVGGSGND TLSGDAGNDV
LEGGAGSDRL TGGEGADIFR FTAVSDSYYT ASSSVADQIL DFDASNDRID LTGLGFTGLG
DGYGGTLAVL ANSDGSRTYL RSYEKDADGR YFSLTLDGNF VGRLDDSNLV FRHKTIAGTE
GDDSLTGNAM AEILDGGSGN DSLAGGLGND VLRGGAGDDI LNGGLGRDQL SGGEGADIFR
FTSVADSYQN SGDNFSDLIL DFDPGEDRID LSGLGFSGLG DGHNGTLLLW TSSETNRTYL
KNFDTDADGR RFEIALEGVF SDLSEKQLVF ERLVLEGTRL GDQLSGTELN EELLGGAGRD
ILNGGAGDDI LDGGSERDTL TGGSGADVFR FNATLDSFRN YDNGTSRVDD ITDFTVGEDL
IDLSALGYSG LGNGYDGTLA VLLNADGTKT YLKDRESDAD GNHFEIALDG NYADQLSNGD
FIFTNLEVIG SSSQAA
