ID   ALGE1_AZOVI    STANDARD;      PRT;  1403 AA.
AC   Q44494;
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 1 (EC 5.1.3.-) (Mannuronan
DE   epimerase 1).
GN   Name=algE1;
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=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   DOMAINS.
RC   STRAIN=E;
RX   MEDLINE=99030352; PubMed=9812987; DOI=10.1074/jbc.273.47.30927;
RA   Ertesvaag H., Hoeidal H.K., Skjaak-Braek G., Valla S.;
RT   "The Azotobacter vinelandii mannuronan C-5-epimerase AlgE1 consists of
RT   two separate catalytic domains.";
RL   J. Biol. Chem. 273:30927-30932(1998).
RN   [3]
RP   DOMAINS.
RC   STRAIN=E;
RX   MEDLINE=99255526; PubMed=10322003;
RA   Ertesvaag H., Valla S.;
RT   "The A modules of the Azotobacter vinelandii mannuronan-C-5-epimerase
RT   AlgE1 are sufficient for both epimerization and binding of Ca2+.";
RL   J. Bacteriol. 181:3033-3038(1999).
RN   [4]
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   [5]
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 two catalytically active A modules and four R
CC       modules. The N-terminal A domain introduces a mixture of MG-blocks
CC       and G- blocks, whereas the C-terminal A domain only generates MG-
CC       blocks.
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 12 hemolysin-type calcium-binding repeats.
CC   -!- SIMILARITY: Contains 15 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; L39096; AAA87311.1; -.
DR   PIR; S77624; S77624.
DR   HSSP; O69771; 1G9K.
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; 12.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00722; CASH; 4.
DR   SMART; SM00710; PbH1; 15.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 9.
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    302       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      697    714       Hemolysin-type calcium-binding 7.
FT   REPEAT      715    732       Hemolysin-type calcium-binding 8.
FT   REPEAT      733    750       Hemolysin-type calcium-binding 9.
FT   REPEAT      977    999       PbH1 8.
FT   REPEAT     1001   1023       PbH1 9.
FT   REPEAT     1024   1046       PbH1 10.
FT   REPEAT     1048   1070       PbH1 11.
FT   REPEAT     1101   1123       PbH1 12.
FT   REPEAT     1124   1146       PbH1 13.
FT   REPEAT     1163   1185       PbH1 14.
FT   REPEAT     1190   1212       PbH1 15.
FT   REPEAT     1226   1243       Hemolysin-type calcium-binding 10.
FT   REPEAT     1244   1261       Hemolysin-type calcium-binding 11.
FT   REPEAT     1262   1279       Hemolysin-type calcium-binding 12.
SQ   SEQUENCE   1403 AA;  147169 MW;  4E843AB0A366A95C CRC64;
     MDYNVKDFGA LGDGVSDDTA AIQAAIDAAH AAGGGTVYLP AGEYRVSGGE EPSDGCLTIK
     SNVHIVGAGM GETVIKMVDG WTQNVTGMVR SAYGEETSNF GMSDLTLDGN RDNLSAKVDG
     WFNGYIPGQD GADRDVTLER VEIREMSGYG FDPHEQTINL TIRDSVAHDN SLDGFVADYQ
     VGGVFENNVS YNNDRHGFNI VTSTNDFVLS NNVAYGNGGA GLVVQRGSYD LPHPYDILID
     GGAYYDNALE GVQLKMAHDV TLQNAEIYGN GLYGVRVYGA QDVQILDNQI HDNSQNGAYA
     EVLLQSYDDT AGVSGNFYVT TGTWLEGNVI SGSANSTYGI QERADGTDYS SLYANSIDGV
     QTGAVRLYGA NSTVSSQSGS GQQATLEGSA GNDALSGTEA HETLLGQAGD DRLNGDAGND
     ILDGGAGRDN LTGGAGADTF RFSARTDSYR TDSASFNDLI TDFDADEDSI DLSALGFTGL
     GDGYNGTLLL KTNAEGTRTY LKSYEADAQG RRFEIALDGN FTGLFNDNNL LFDAAPATGT
     EGSDNLLGTD AGETLLGYGG NDTLNGGAGD DILVGGAGRD SLTGGAGADV FRFDALSDSQ
     RNYTTGDNQA DRILDFDPTL DRIDVSALGF TGLGNGRNGT LAVVLNSAGD RTDLKSYDTD
     ANGYSFELSL AGNYQGQLSA EQFVFATSQG GQMTIIEGTD GNDTLQGTEA NERLLGLDGR
     DNLNGGAGDD ILDGGAGRDT LTGGTGADTF LFSTRTDSYR TDSASFNDLI TDFDPTQDRI
     DLSGLGFSGF GNGYDGTLLL QVNAAGTRTY LKSFEADANG QRFEIALDGD FSGQLDSGNV
     IFEPAVFNAK DFGALGDGAS DDRPAIQAAI DAAYAAGGGT VYLPAGEYRV SPTGEPGDGC
     LMLKDGVYLA GDGIGETVIK LIDGSDQKIT GMVRSAYGEE TSNFGMSDLT LDGNRDNTSG
     KVDGWFNGYI PGQDGADRNV TIERVEIREM SGYGFDPHEQ TINLTIRDSV AHDNGLDGFV
     ADYLVDSVFE NNVAYNNDRH GFNIVTSTYD FVMTNNVAYG NGGAGLTIQR GSEDLAQPTD
     ILIDGGAYYD NALEGVLFKM TNNVTLQNAE IYGNGSSGVR LYGTEDVQIL DNQIHDNSQN
     GTYPEVLLQA FDDSQVTGEL YETLNTRIEG NLIDASDNAN YAVRERDDGS DYTTLVDNDI
     SGGQVASVQL SGAHSSLSGG TVEVPQGTDG NDVLVGSDAN DQLYGGAGDD RLDGGAGDDL
     LDGGAGRDDL TGGTGADTFV FAARTDSYRT DAGVFNDLIL DFDASEDRID LSALGFSGFG
     DGYNGTLLVQ LSSAGTRTYL KSYEEDLEGR RFEVALDGDH TGDLSAANVV FADDGSAAVA
     SSDPAATQLE VVGSSGTQTD QLA
//