ID   ALGE6_AZOVI    STANDARD;      PRT;   874 AA.
AC   Q9ZFH0;
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 6 (EC 5.1.3.-) (Mannuronan
DE   epimerase 6).
GN   Name=algE6;
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   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), producing a polymer with gel-forming capacity, required
CC       for the formation of the cyst coat.
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 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
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 8 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; AF099799; AAD04920.1; -.
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      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    302       PbH1 7.
FT   REPEAT      320    351       PbH1 8.
FT   REPEAT      382    399       Hemolysin-type calcium-binding 1.
FT   REPEAT      400    417       Hemolysin-type calcium-binding 2.
FT   REPEAT      418    435       Hemolysin-type calcium-binding 3.
FT   REPEAT      561    578       Hemolysin-type calcium-binding 4.
FT   REPEAT      579    596       Hemolysin-type calcium-binding 5.
FT   REPEAT      704    721       Hemolysin-type calcium-binding 6.
FT   REPEAT      722    739       Hemolysin-type calcium-binding 7.
FT   REPEAT      740    757       Hemolysin-type calcium-binding 8.
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
//