ALGE4_AZOVI
ID ALGE4_AZOVI Reviewed; 553 AA.
AC Q44493;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Mannuronan C5-epimerase AlgE4 {ECO:0000305};
DE EC=5.1.3.37 {ECO:0000269|PubMed:10212201};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase 4;
GN Name=algE4 {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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=E;
RX PubMed=10212201; DOI=10.1074/jbc.274.18.12316;
RA Hoeidal H.K., Ertesvaag H., Skjaak-Braek G., Stokke B.T., Valla S.;
RT "The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4
RT epimerizes alginate by a nonrandom attack mechanism.";
RL J. Biol. Chem. 274:12316-12322(1999).
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), but introduces almost exclusively MG blocks, producing a polymer
CC with non-gel-forming capacity. {ECO:0000269|PubMed:10212201}.
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:10212201};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10212201};
CC -!- ACTIVITY REGULATION: Inhibited by zinc. {ECO:0000269|PubMed:10212201}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=14.8 umol/min/mg enzyme {ECO:0000269|PubMed:10212201};
CC Note=kcat is 14 sec(-1). {ECO:0000269|PubMed:10212201};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:10212201};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:10212201};
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis. {ECO:0000305}.
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 one R module.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L39096; AAA87310.1; -; Genomic_DNA.
DR PIR; S77623; S77623.
DR PDB; 2AGM; NMR; -; A=387-553.
DR PDB; 2PYG; X-ray; 2.10 A; A/B=1-377.
DR PDB; 2PYH; X-ray; 2.70 A; A/B=1-377.
DR PDBsum; 2AGM; -.
DR PDBsum; 2PYG; -.
DR PDBsum; 2PYH; -.
DR AlphaFoldDB; Q44493; -.
DR BMRB; Q44493; -.
DR SMR; Q44493; -.
DR BioCyc; MetaCyc:MON-14389; -.
DR BRENDA; 5.1.3.37; 49.
DR UniPathway; UPA00286; -.
DR EvolutionaryTrace; Q44493; -.
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; 2.160.20.10; -; 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; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00353; HemolysinCabind; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SMART; SM00722; CASH; 2.
DR SMART; SM00710; PbH1; 8.
DR SUPFAM; SSF51120; SSF51120; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alginate biosynthesis; Calcium; Isomerase; Repeat; Secreted.
FT CHAIN 1..553
FT /note="Mannuronan C5-epimerase AlgE4"
FT /id="PRO_0000219558"
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..301
FT /note="PbH1 7"
FT /evidence="ECO:0000255"
FT REPEAT 320..342
FT /note="PbH1 8"
FT /evidence="ECO:0000255"
FT REPEAT 403..420
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 421..438
FT /note="Hemolysin-type calcium-binding 2"
FT REGION 367..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2PYG"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2PYG"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:2PYG"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 174..187
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2PYH"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 251..264
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 274..287
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 356..365
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:2PYG"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 428..434
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:2AGM"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 494..502
FT /evidence="ECO:0007829|PDB:2AGM"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:2AGM"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:2AGM"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:2AGM"
SQ SEQUENCE 553 AA; 57709 MW; 2806B4AEA3FFF128 CRC64;
MDYNVKDFGA LGDGVSDDRA SIQAAIDAAY AAGGGTVYLP AGEYRVSAAG EPGDGCLMLK
DGVYLAGAGM GETVIKLIDG SDQKITGMVR SAYGEETSNF GMRDLTLDGN RDNTSGKVDG
WFNGYIPGGD GADRDVTIER VEVREMSGYG FDPHEQTINL TIRDSVAHDN GLDGFVADYL
VDSVFENNVA YANDRHGFNV VTSTHDFVMT NNVAYGNGSS GLVVQRGLED LALPSNILID
GGAYYDNARE GVLLKMTSDI TLQNADIHGN GSSGVRVYGA QDVQILDNQI HDNAQAAAVP
EVLLQSFDDT AGASGTYYTT LNTRIEGNTI SGSANSTYGI QERNDGTDYS SLIDNDIAGV
QQPIQLYGPH STVSGEPGAT PQQPSTGSDG EPLVGGDTDD QLQGGSGADR LDGGAGDDIL
DGGAGRDRLS GGAGADTFVF SAREDSYRTD TAVFNDLILD FEASEDRIDL SALGFSGLGD
GYGGTLLLKT NAEGTRTYLK SFEADAEGRR FEVALDGDHT GDLSAANVVF AATGTTTELE
VLGDSGTQAG AIV
