ID ALGE7_AZOVI STANDARD; PRT; 856 AA. AC Q9ZFG9; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 21-MAR-2006, entry version 34. DE Poly(beta-D-mannuronate) C5 epimerase 7 (EC 5.1.3.-) (Mannuronan DE epimerase 7). GN Name=algE7; OS Azotobacter vinelandii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 CHARACTERIZATION, AND MUTAGENESIS OF ASP-152. RC STRAIN=E; RX MEDLINE=21402877; PubMed=11390391; DOI=10.1074/jbc.M102562200; RA Glaerum Svanem B.I., Strand W.I., Ertesvaag H., Skjaak-Braek G., RA Hartmann M., Barbeyron T., Valla S.; RT "The catalytic activities of the bifunctional Azotobacter vinelandii RT mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate RT from the same active site in the enzyme."; RL J. Biol. Chem. 276:31542-31550(2001). 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). Has both epimerase and lyase activities. Contributes to CC abortive encystment by degrading the coat from inside the cyst. CC Important for cyst germination. 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 germinating 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 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 8 hemolysin-type calcium-binding repeats. CC -!- SIMILARITY: Contains 9 PbH1 repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF099800; AAD04921.1; -; Genomic_DNA. DR InterPro; IPR006633; CASH. DR InterPro; IPR001343; Hemlysn_Ca_bd. DR InterPro; IPR006626; PbH1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011049; Serralysn_like_C. DR InterPro; IPR011050; Virulence_PecLys. DR Pfam; PF00353; HemolysinCabind; 8. DR PRINTS; PR00313; CABNDNGRPT. DR SMART; SM00722; CASH; 1. DR SMART; SM00710; PbH1; 1. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6. KW Alginate biosynthesis; Calcium; Isomerase; Repeat. FT CHAIN 1 856 Poly(beta-D-mannuronate) C5 epimerase 7. FT /FTId=PRO_0000219561. FT REPEAT 97 125 PbH1 1. FT REPEAT 133 155 PbH1 2. FT REPEAT 157 179 PbH1 3. FT REPEAT 180 202 PbH1 4. FT REPEAT 204 226 PbH1 5. FT REPEAT 234 256 PbH1 6. FT REPEAT 257 279 PbH1 7. FT REPEAT 280 304 PbH1 8. FT REPEAT 320 342 PbH1 9. FT REPEAT 386 403 Hemolysin-type calcium-binding 1. FT REPEAT 404 421 Hemolysin-type calcium-binding 2. FT REPEAT 422 439 Hemolysin-type calcium-binding 3. FT REPEAT 537 554 Hemolysin-type calcium-binding 4. FT REPEAT 555 572 Hemolysin-type calcium-binding 5. FT REPEAT 573 590 Hemolysin-type calcium-binding 6. FT REPEAT 714 731 Hemolysin-type calcium-binding 7. FT REPEAT 732 749 Hemolysin-type calcium-binding 8. FT MUTAGEN 152 152 D->G: Loss of both epimerase and lyase FT functions. SQ SEQUENCE 856 AA; 90364 MW; 626DDCA4681E8807 CRC64; MEYNVKDFGA KGDGKTDDTD AIQAAIDAAH KAGGGTVYLP SGEYRVSGGD EASDGALIIK SNVYIVGAGM GETVIKLVDG WDEKLTGIIR SANGEKTHDY GISDLTIDGN QDNTEGEVDG FYTGYIPGKN GADYNVTVER VEIREVSRYA FDPHEQTINL TIRDSVAHDN GKDGFVADFQ IGAVFENNVS YNNGRHGFNI VTSSHDIVFT NNVAYGNGAN GLVVQRGSED RDFVYNVEIE GGSFHDNGQE GVLIKMSTDV TLQGAEIYGN GYAGVRVQGV EDVRILDNYI HDNAQSKANA EVIVESYDDR DGPSDDYYET QNVTVKGNTI VGSANSTYGI QERADGTDYT SIGNNSVSGT QRGIVQLSGT NSTFSGRSGD AYQFIDGSTG NDLLTGTPIA DLIVGGSGND TLSGDAGNDV LEGGAGSDRL TGGEGADIFR FTAVSDSYYT ASSSVADQIL DFDASNDRID LTGLGFTGLG DGYGGTLAVL ANSDGSRTYL RSYEKDADGR YFSLTLDGNF VGRLDDSNLV FRHKTIAGTE GDDSLTGNAM AEILDGGSGN DSLAGGLGND VLRGGAGDDI LNGGLGRDQL SGGEGADIFR FTSVADSYQN SGDNFSDLIL DFDPGEDRID LSGLGFSGLG DGHNGTLLLW TSSETNRTYL KNFDTDADGR RFEIALEGVF SDLSEKQLVF ERLVLEGTRL GDQLSGTELN EELLGGAGRD ILNGGAGDDI LDGGSERDTL TGGSGADVFR FNATLDSFRN YDNGTSRVDD ITDFTVGEDL IDLSALGYSG LGNGYDGTLA VLLNADGTKT YLKDRESDAD GNHFEIALDG NYADQLSNGD FIFTNLEVIG SSSQAA //