ID   ALGE2_AZOVI    STANDARD;      PRT;   997 AA.
AC   Q44495;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   21-MAR-2006, entry version 34.
DE   Poly(beta-D-mannuronate) C5 epimerase 2 (EC 5.1.3.-) (Mannuronan
DE   epimerase 2).
GN   Name=algE2;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RC   STRAIN=E;
RX   MEDLINE=94245609; PubMed=8188585;
RA   Ertesvaag H., Doseth B., Larsen B., Skjaak-Braek G., Valla S.;
RT   "Cloning and expression of an Azotobacter vinelandii mannuronan
RT   C-5-epimerase gene.";
RL   J. Bacteriol. 176:2846-2853(1994).
RN   [2]
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   [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), 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: Secreted protein; extracellular space.
CC       Probably exported via the hemolysin-type secretion pathway.
CC   -!- DEVELOPMENTAL STAGE: Produced mainly in 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
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 11 hemolysin-type calcium-binding repeats.
CC   -!- SIMILARITY: Contains 7 PbH1 repeats.
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DR   EMBL; L39096; AAA87312.1; -; Genomic_DNA.
DR   PIR; S77625; S77625.
DR   InterPro; IPR006633; CASH.
DR   InterPro; IPR001343; Hemlysn_Ca_bd.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR003995; RtxA.
DR   InterPro; IPR011049; Serralysn_like_C.
DR   InterPro; IPR011050; Virulence_PecLys.
DR   Pfam; PF00353; HemolysinCabind; 11.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   PRINTS; PR01488; RTXTOXINA.
DR   SMART; SM00722; CASH; 2.
DR   SMART; SM00710; PbH1; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
KW   Alginate biosynthesis; Calcium; Direct protein sequencing; Isomerase;
KW   Repeat.
FT   CHAIN         1    997       Poly(beta-D-mannuronate) C5 epimerase 2.
FT                                /FTId=PRO_0000219556.
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      695    712       Hemolysin-type calcium-binding 7.
FT   REPEAT      713    730       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;  103084 MW;  B3D3C1E57ADAC404 CRC64;
     MDYNVKDFGA LGDGVSDDTA AIQAAIDAAY AAGGGTVYLP AGEYRVSGGE EPSDGCLTIK
     SNVHIVGAGM GETVIKLVDG WDQDVTGIVR SAYGEETSNF GMSDLTLDGN RDNTSGKVDG
     WFNGYIPGED GADRDVTLER VEIREMSGYG FDPHEQTINL TIRDSVAHDN GLDGFVADFQ
     IGGVFENNVS YNNDRHGFNI VTSTNDFVLS NNVAYGNGGA GLVVQRGSSD VAHPYDILID
     GGAYYDNGLE GVQIKMAHDV TLQNAEIYGN GLYGVRVYGA EDVQILDNYI HDNSQNGSYA
     EILLQSYDDT AGVSGNFYTT TGTWIEGNTI VGSANSTYGI QERDDGTDYS SLYANSVSNV
     QNGSVRLYGA NSVVSDLPGT GQQATLEGTA GNDTLGGSDA HETLLGLDGN DRLNGGAGND
     ILDGGAGRDN LTGGAGADLF RVSARTDSYR TDSASFNDLI TDFDASQDRI DLSALGFTGL
     GDGYNGTLLL QVSADGSRTY LKSLEADAEG RRFEIALDGN FAGLLGAGNL LFERTAIEGD
     AGDNALLGTS AAETLLGHAG NDTLDGGAGD DILVGGAGRD SLTGGAGADV FRFDALSDSQ
     RNYDIGDNQG DRIADFAVGE DKLDVSALGF TGLGDGYNGT LALVLNSAGD RTYVKSYENG
     ADGYRFEFSL DGNYLELLGN EDFIFATPSG QQLLEGSAGN DSLQGTAADE VIHGGGGRDT
     LAGGAGADVF RFSELTDSYR DSASYADLIT DFDASEDRID LSGLGFSGLG NGYGGTLALQ
     VNSAGTRTYL KSFETNAAGE RFEIALDGDL SALGGANLIL DARTVLAGGD GNDTLSGSSA
     AEELLGGVGN DSLDGGAGND ILDGGAGRDT LSGGSGSDIF RFGGALDSFR NYASGTNGTD
     SITDFTPGED LIDLSVLGYT GLGDGYNGTL AIVLNDAGTK TYLKNRESDA EGNQFEIALE
     GNHADQLDAS DFIFATAAAT TGIEVVGGSG TQTDQLA
//