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 25-MAY-2022, entry version 102.
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; Proteobacteria; 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; -; 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 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
