ID   ALGE5_AZOVI    STANDARD;      PRT;   997 AA.
AC   Q44492;
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 5 (EC 5.1.3.-) (Mannuronan
DE   epimerase 5).
GN   Name=algE5;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E;
RX   PubMed=7476166;
RA   Ertesvag H., Hoidal 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   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 during vegetative growth and in
CC       encysting cells.
CC   -!- DOMAIN: Composed of one catalytically active A module and four 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 11 hemolysin-type calcium-binding repeats.
CC   -!- SIMILARITY: Contains 7 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; L39013; AAA87309.1; -.
DR   PIR; I39739; I39739.
DR   InterPro; IPR006633; CASH.
DR   InterPro; IPR001343; Hemlysn_Ca_bind.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR011050; Pectin_lyas_like.
DR   InterPro; IPR003995; RtxA.
DR   InterPro; IPR011049; Serralysn_like_C.
DR   Pfam; PF00353; HemolysinCabind; 11.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   PRINTS; PR01488; RTXTOXINA.
DR   SMART; SM00722; CASH; 2.
DR   SMART; SM00710; PbH1; 7.
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      257    279       PbH1 5.
FT   REPEAT      280    315       PbH1 6.
FT   REPEAT      320    359       PbH1 7.
FT   REPEAT      387    404       Hemolysin-type calcium-binding 1.
FT   REPEAT      405    422       Hemolysin-type calcium-binding 2.
FT   REPEAT      423    440       Hemolysin-type calcium-binding 3.
FT   REPEAT      538    555       Hemolysin-type calcium-binding 4.
FT   REPEAT      556    573       Hemolysin-type calcium-binding 5.
FT   REPEAT      574    591       Hemolysin-type calcium-binding 6.
FT   REPEAT      694    711       Hemolysin-type calcium-binding 7.
FT   REPEAT      712    729       Hemolysin-type calcium-binding 8.
FT   REPEAT      827    844       Hemolysin-type calcium-binding 9.
FT   REPEAT      845    862       Hemolysin-type calcium-binding 10.
FT   REPEAT      863    880       Hemolysin-type calcium-binding 11.
SQ   SEQUENCE   997 AA;  103724 MW;  76C3E05504DCFB99 CRC64;
     MDYNVKDFGA LGDGVSDDTA AIQAAIDAAY AAGGGTVYLP AGEYRVSGGE EPSDGCLTIK
     SNVYIVGAGM GETVIKLVDG WDQDVTGIVR SAYGEETSNF GMSDLTLDGN RDNTSGKVDG
     WFNGYIPGED GADRDVTLER VEIREMSGYG FDPHEQTINL TIRDSVAHDN GLDGFVADFQ
     IGGVFENNVS YNNDRHGFNI VTSTNDFVLS NNVAYGNGGA GLVIQRGSYD VAHPYGILID
     GGAYYDNGLE GVQIKMAHDV TLQNAEIYGN GLYGVRVYGA EDVQILDNYI HDNSQSGSYA
     EILLQSYDDT AGVSGNFYTT TGTWIEGNTI VGSANSTYGI QERADGTDYS SLYANSVSNV
     QSGSVRLYGT NSVVSDLPGT GQQATLEGTT GNDTLTGSEA HETLLGLDGN DRLNGGAGND
     ILDGGAGRDN LTGGAGADLF RVSARTDSYR TDSASFNDLI TDFDPAQDRI DLSALGFTGL
     GDGYNGTLAV VLNSAGTRTY LKSYEADAEG RRFEIALDGN FAGLLDDGNL IFERPVIEGD
     AGNNALLGTS AAETLLGHAG NDTLDGAGGD DILVGGAGRD TLTGGAGADL FRFDALSDSQ
     RNYTTGDNQG DRIVDFSVGE DKLDVSALGF TGLGDGYNGT LAVVVNSAGD RTYVKSYETD
     ADGYRFEFSL EGNYQDLGSE SFVFATPSGQ QLLEGSAGND SLQGTAADEI VHGGAGRDTL
     SGGAGADVFR FSELTDSYRT ASTSFADLIT DFDLADDRID LSGLGFSGLG DGYDGTLAVV
     VNSTGTRTYL KSYEANAAGE RFEIALDGDL SAFTGANLIL DERVVLEGSD GNDTLDGGSA
     AEELLGGAGN DSLDGGAGND ILDGGAGRDT LSGGSGSDIF RYDDALDSFR NYGTGVTGTD
     TITDFTPGED LIDLSALGYT GLGDGYNGTL AVVLNGDGTR TYLKDRESDA EGNQFEIALD
     GDLVDRLDAG DFIFAEAAAT TAIEVVGGTP TEEQLVA
//