ID   ALGE4_AZOVI    STANDARD;      PRT;   553 AA.
AC   Q44493;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   21-MAR-2006, entry version 35.
DE   Poly(beta-D-mannuronate) C5 epimerase 4 (EC 5.1.3.-) (Mannuronan
DE   epimerase 4).
GN   Name=algE4;
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   MEDLINE=96065700; PubMed=7476166;
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
RT   alginate structure in Azotobacter vinelandii.";
RL   Mol. Microbiol. 16:719-731(1995).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=E;
RX   MEDLINE=99230244; 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   MEDLINE=21132699; PubMed=11243259;
RX   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   MEDLINE=20391728; PubMed=10937941; DOI=10.1006/mben.1999.0130;
RA   Ertesvaag H., Hoeidal H.K., Schjerven H., Glaerum Svanem B.I.,
RA   Valla S.;
RT   "Mannuronan C-5-epimerases and their application for in vitro and in
RT   vivo 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
CC       acid (G), but introduces almost exclusively MG blocks, producing a
CC       polymer with non-gel-forming capacity.
CC   -!- COFACTOR: Calcium.
CC   -!- ENZYME REGULATION: Inhibited by zinc.
CC   -!- PATHWAY: Alginate biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Secreted protein; extracellular space.
CC       Probably exported via the hemolysin-type secretion pathway.
CC   -!- DEVELOPMENTAL STAGE: Produced in encysting cells.
CC   -!- DOMAIN: Composed of one catalytically active A module and one R
CC       module.
CC   -!- MISCELLANEOUS: Each enzyme of this family of C5 epimerases
CC       introduces its own characteristic sequence distribution of
CC       G-blocks in their substrates, explaining the extensive sequence
CC       variability of alginates. These alginates of varying composition
CC       have different physical properties and are necessary at different
CC       stages of the bacterium life cycle.
CC   -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC   -!- SIMILARITY: Contains 2 hemolysin-type calcium-binding repeats.
CC   -!- SIMILARITY: Contains 8 PbH1 repeats.
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DR   EMBL; L39096; AAA87310.1; -; Genomic_DNA.
DR   PIR; S77623; S77623.
DR   PDB; 2AGM; NMR; A=387-553.
DR   InterPro; IPR006633; CASH.
DR   InterPro; IPR001343; Hemlysn_Ca_bd.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011049; Serralysn_like_C.
DR   InterPro; IPR011050; Virulence_PecLys.
DR   Pfam; PF00353; HemolysinCabind; 2.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00722; CASH; 2.
DR   SMART; SM00710; PbH1; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 3.
KW   3D-structure; Alginate biosynthesis; Calcium; Isomerase; Repeat.
FT   CHAIN         1    553       Poly(beta-D-mannuronate) C5 epimerase 4.
FT                                /FTId=PRO_0000219558.
FT   REPEAT      133    155       PbH1 1.
FT   REPEAT      157    179       PbH1 2.
FT   REPEAT      180    202       PbH1 3.
FT   REPEAT      204    226       PbH1 4.
FT   REPEAT      234    256       PbH1 5.
FT   REPEAT      257    279       PbH1 6.
FT   REPEAT      280    301       PbH1 7.
FT   REPEAT      320    342       PbH1 8.
FT   REPEAT      403    420       Hemolysin-type calcium-binding 1.
FT   REPEAT      421    438       Hemolysin-type calcium-binding 2.
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
//