ALGE6_AZOVI
ID ALGE6_AZOVI Reviewed; 874 AA.
AC Q9ZFH0;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Mannuronan C5-epimerase AlgE6 {ECO:0000305};
DE EC=5.1.3.37 {ECO:0000269|PubMed:9864314};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase 6;
GN Name=algE6 {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 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:9864314}.
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};
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 in encysting 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; AF099799; AAD04920.1; -; Genomic_DNA.
DR PDB; 2ML1; NMR; -; A=382-532.
DR PDB; 2ML2; NMR; -; A=534-694.
DR PDB; 2ML3; NMR; -; A=695-872.
DR PDB; 5LW3; X-ray; 1.19 A; A=1-385.
DR PDBsum; 2ML1; -.
DR PDBsum; 2ML2; -.
DR PDBsum; 2ML3; -.
DR PDBsum; 5LW3; -.
DR AlphaFoldDB; Q9ZFH0; -.
DR BMRB; Q9ZFH0; -.
DR SMR; Q9ZFH0; -.
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; -; 2.
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; 3.
DR Pfam; PF12708; Pectate_lyase_3; 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 3D-structure; Alginate biosynthesis; Calcium; Isomerase; Repeat; Secreted.
FT CHAIN 1..874
FT /note="Mannuronan C5-epimerase AlgE6"
FT /id="PRO_0000219560"
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..302
FT /note="PbH1 7"
FT /evidence="ECO:0000255"
FT REPEAT 320..351
FT /note="PbH1 8"
FT /evidence="ECO:0000255"
FT REPEAT 383..394
FT /note="Hemolysin-type calcium-binding 1"
FT /evidence="ECO:0000255"
FT REPEAT 401..417
FT /note="Hemolysin-type calcium-binding 2"
FT /evidence="ECO:0000255"
FT REPEAT 419..435
FT /note="Hemolysin-type calcium-binding 3"
FT /evidence="ECO:0000255"
FT REPEAT 562..578
FT /note="Hemolysin-type calcium-binding 4"
FT /evidence="ECO:0000255"
FT REPEAT 580..596
FT /note="Hemolysin-type calcium-binding 5"
FT /evidence="ECO:0000255"
FT REPEAT 723..739
FT /note="Hemolysin-type calcium-binding 6"
FT /evidence="ECO:0000255"
FT REPEAT 741..757
FT /note="Hemolysin-type calcium-binding 7"
FT /evidence="ECO:0000255"
FT REGION 401..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:5LW3"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:5LW3"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:5LW3"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:5LW3"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 356..365
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:5LW3"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:2ML1"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:2ML1"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:2ML1"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:2ML1"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:2ML1"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:2ML2"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 614..618
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:2ML2"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:2ML2"
FT TURN 650..653
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 654..658
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 663..666
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 668..675
FT /evidence="ECO:0007829|PDB:2ML2"
FT TURN 677..680
FT /evidence="ECO:0007829|PDB:2ML2"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:2ML2"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 776..779
FT /evidence="ECO:0007829|PDB:2ML3"
FT TURN 782..784
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:2ML3"
FT TURN 790..793
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 801..804
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 807..814
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 816..823
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 829..836
FT /evidence="ECO:0007829|PDB:2ML3"
FT HELIX 839..841
FT /evidence="ECO:0007829|PDB:2ML3"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:2ML3"
SQ SEQUENCE 874 AA; 90160 MW; 22487F3A445427F1 CRC64;
MDYNVKDFGA LGDGVSDDRV AIQAAIDAAH AAGGGTVYLP PGEYRVSAAG EPSDGCLTLR
DNVYLAGAGM GQTVIKLVDG SAQKITGIVR SPFGEETSNF GMRDLTLDGN RANTVDKVDG
WFNGYAPGQP GADRNVTIER VEVREMSGYG FDPHEQTINL VLRDSVAHHN GLDGFVADYQ
IGGTFENNVA YANDRHGFNI VTSTNDFVMR NNVAYGNGGN GLVVQRGSEN LAHPENILID
GGSYYDNGLE GVLVKMSNNV TVQNADIHGN GSSGVRVYGA QGVQILGNQI HDNAKTAVAP
EVLLQSYDDT LGVSGNYYTT LNTRVEGNTI TGSANSTYGV QERNDGTDFS SLVGNTINGV
QEAAHLYGPN STVSGTVSAP PQGTDGNDVL IGSDVGEQIS GGAGDDRLDG GAGDDLLDGG
AGRDRLTGGL GADTFRFALR EDSHRSPLGT FSDLILDFDP SQDKIDVSAL GFIGLGNGYA
GTLAVSLSAD GLRTYLKSYD ADAQGRSFEL ALDGNHAATL SAGNIVFAAA TPVDPSAEAQ
PIVGSDLDDQ LHGTLLGEEI SGGGGADQLY GYGGGDLLDG GAGRDRLTGG EGADTFRFAL
REDSHRSAAG TFSDLILDFD PTQDKLDVSA LGFTGLGNGY AGTLAVSVSD DGTRTYLKSY
ETDAEGRSFE VSLQGNHAAA LSADNILFAT PVPVDPGVEG TPVVGSDLDD ELHGTLGSEQ
ILGGGGADQL YGYAGNDLLD GGAGRDKLSG GEGADTFRFA LREDSHRSPL GTFGDRILDF
DPSQDRIDVS ALGFSGLGNG YAGSLAVSVS DDGTRTYLKS YEADAQGLSF EVALEGDHAA
ALSADNIVFA ATDAAAAGEL GVIGASGQPD DPAV
