ID   ALGE7_AZOVI    STANDARD;      PRT;   856 AA.
AC   Q9ZFG9;
DT   10-OCT-2003 (Rel. 42, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Poly(beta-D-mannuronate) C5 epimerase 7 (EC 5.1.3.-) (Mannuronan
DE   epimerase 7).
GN   Name=algE7;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E;
RX   MEDLINE=99084941; PubMed=9864314;
RA   Glaerum Svanem B.I., Skjaak-Braek G., Ertesvaag H., Valla S.;
RT   "Cloning and expression of three new Azotobacter vinelandii genes
RT   closely related to a previously described gene family encoding
RT   mannuronan C-5-epimerases.";
RL   J. Bacteriol. 181:68-77(1999).
RN   [2]
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   [3]
RP   CHARACTERIZATION, AND MUTAGENESIS OF ASP-152.
RC   STRAIN=E;
RX   MEDLINE=21402877; 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
RT   from the same active site in the enzyme.";
RL   J. Biol. Chem. 276:31542-31550(2001).
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). Has both epimerase and lyase activities. Contributes to
CC       abortive encystment by degrading the coat from inside the cyst.
CC       Important for cyst germination.
CC   -!- COFACTOR: Calcium.
CC   -!- ENZYME REGULATION: Inhibited by zinc.
CC   -!- PATHWAY: Alginate biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Extracellular. 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
CC       introduces its own characteristic sequence distribution of G-
CC       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 8 hemolysin-type calcium-binding repeats.
CC   -!- SIMILARITY: Contains 9 PbH1 repeats.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AF099800; AAD04921.1; -.
DR   InterPro; IPR006633; CASH.
DR   InterPro; IPR001343; Hemlysn_Ca_bind.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR011050; Pectin_lyas_like.
DR   InterPro; IPR011049; Serralysn_like_C.
DR   Pfam; PF00353; HemolysinCabind; 8.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00722; CASH; 2.
DR   SMART; SM00710; PbH1; 8.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
KW   Alginate biosynthesis; Calcium; Isomerase; Multigene family; Repeat.
FT   REPEAT       97    125       PbH1 1.
FT   REPEAT      133    155       PbH1 2.
FT   REPEAT      157    179       PbH1 3.
FT   REPEAT      180    202       PbH1 4.
FT   REPEAT      204    226       PbH1 5.
FT   REPEAT      234    256       PbH1 6.
FT   REPEAT      257    279       PbH1 7.
FT   REPEAT      280    304       PbH1 8.
FT   REPEAT      320    342       PbH1 9.
FT   REPEAT      386    403       Hemolysin-type calcium-binding 1.
FT   REPEAT      404    421       Hemolysin-type calcium-binding 2.
FT   REPEAT      422    439       Hemolysin-type calcium-binding 3.
FT   REPEAT      537    554       Hemolysin-type calcium-binding 4.
FT   REPEAT      555    572       Hemolysin-type calcium-binding 5.
FT   REPEAT      573    590       Hemolysin-type calcium-binding 6.
FT   REPEAT      714    731       Hemolysin-type calcium-binding 7.
FT   REPEAT      732    749       Hemolysin-type calcium-binding 8.
FT   MUTAGEN     152    152       D->G: Loss of both epimerase and lyase
FT                                functions.
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
//