ID   ALGG_AZOVI     STANDARD;      PRT;   525 AA.
AC   P70805;
DT   10-OCT-2003 (Rel. 42, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Poly(beta-D-mannuronate) C5 epimerase precursor (EC 5.1.3.-).
GN   Name=algG;
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=96427318; PubMed=8830682;
RA   Rehm B.H.A., Ertesvaag H., Valla S.;
RT   "A new Azotobacter vinelandii mannuronan C-5-epimerase gene (algG) is
RT   part of an alg gene cluster physically organized in a manner similar
RT   to that in Pseudomonas aeruginosa.";
RL   J. Bacteriol. 178:5884-5889(1996).
CC   -!- FUNCTION: Bifunctional protein that converts poly(beta-D-
CC       mannuronate) to alpha-L-guluronate and that is also part of a
CC       periplasmic protein complex that serves as a scaffold that leads
CC       the newly formed alginate polymer through the periplasmic space to
CC       the outer membrane secretin algE (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by zinc.
CC   -!- PATHWAY: Alginate biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Periplasmic (Potential).
CC   -!- DEVELOPMENTAL STAGE: Produced during vegetative growth.
CC   -!- MISCELLANEOUS: This epimerase does not require calcium for its
CC       activity. Probably cannot form G- blocks.
CC   -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC   -!- SIMILARITY: Contains 5 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; X87973; CAA61231.1; -.
DR   InterPro; IPR006633; CASH.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR011050; Pectin_lyas_like.
DR   SMART; SM00722; CASH; 1.
DR   SMART; SM00710; PbH1; 5.
KW   Alginate biosynthesis; Isomerase; Periplasmic; Repeat; Signal.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30    525       Poly(beta-D-mannuronate) C5 epimerase.
FT   REPEAT      287    309       PbH1 1.
FT   REPEAT      311    334       PbH1 2.
FT   REPEAT      336    358       PbH1 3.
FT   REPEAT      360    382       PbH1 4.
FT   REPEAT      383    405       PbH1 5.
SQ   SEQUENCE   525 AA;  58317 MW;  9F9DC15A318CDF3C CRC64;
     MNVQRKLAST QLKPVLLGVL LATSAWSQAA PPEQARQSAP PTLSSKQYSV TSASIEALKL
     DPPKLPDLSG YTHAAVEAKI RRKPGGRIAA AMLQQTALKD FTGGSGRLRE WIVRQGGMPH
     AIFIEGGYVE LGQLARQLPA NQFAETTPGV YVARVPIVVA PGATLHIGKN VKELRLSEER
     GAFLVNDGKL FITDTKLVGW SEKNNAPSAY RGPESFWAFL VSWGGTETYI SRRPVASLGY
     NTSKAYGVSI TQYTPEMHKR LKRPRPTGWL IDSVFEDIYY GFYCYEADDV VLKGNTYRDN
     IIYGIDPHDR SERLVIAENH VYGTKKKHGI IVSREVNNSW IINNRTHDNK LSGIVLDRNS
     EHNLVAYNEV YQNHSDGITL YESSNNLIWG NRLINNARHG IRMRNSVNIR IYENLSVVNQ
     LTGIYGHIKD LSSTDRDFKL DPFDTKVSMI VVGGQLTGNG SSPISVDSPL SLELYRVEML
     APTKSSGLTF TGILEDKQEE ILDLLVRRQK AVLIDPVVDL AQAEL
//