ID ALGE4_AZOVI STANDARD; PRT; 553 AA. AC Q44493; 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 4 (EC 5.1.3.-) (Mannuronan DE epimerase 4). GN Name=algE4; 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 CHARACTERIZATION. RC STRAIN=E; RX MEDLINE=99230244; PubMed=10212201; DOI=10.1074/jbc.274.18.12316; RA Hoeidal H.K., Ertesvaag H., Skjaak-Braek G., Stokke B.T., Valla S.; RT "The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 RT epimerizes alginate by a nonrandom attack mechanism."; RL J. Biol. Chem. 274:12316-12322(1999). 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), but introduces almost exclusively MG blocks, producing a CC polymer with non-gel-forming capacity. 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 in encysting cells. CC -!- DOMAIN: Composed of one catalytically active A module and one R CC module. 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 2 hemolysin-type calcium-binding repeats. CC -!- SIMILARITY: Contains 8 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; AAA87310.1; -. DR PIR; S77623; S77623. DR InterPro; IPR006633; CASH. DR InterPro; IPR001343; Hemlysn_Ca_bind. DR InterPro; IPR006626; PbH1. DR InterPro; IPR011050; Pectin_lyas_like. DR Pfam; PF00353; HemolysinCabind; 2. DR PRINTS; PR00313; CABNDNGRPT. DR SMART; SM00722; CASH; 2. DR SMART; SM00710; PbH1; 8. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 3. 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 234 256 PbH1 5. FT REPEAT 257 279 PbH1 6. FT REPEAT 280 301 PbH1 7. FT REPEAT 320 342 PbH1 8. FT REPEAT 403 420 Hemolysin-type calcium-binding 1. FT REPEAT 421 438 Hemolysin-type calcium-binding 2. SQ SEQUENCE 553 AA; 57709 MW; 2806B4AEA3FFF128 CRC64; MDYNVKDFGA LGDGVSDDRA SIQAAIDAAY AAGGGTVYLP AGEYRVSAAG EPGDGCLMLK DGVYLAGAGM GETVIKLIDG SDQKITGMVR SAYGEETSNF GMRDLTLDGN RDNTSGKVDG WFNGYIPGGD GADRDVTIER VEVREMSGYG FDPHEQTINL TIRDSVAHDN GLDGFVADYL VDSVFENNVA YANDRHGFNV VTSTHDFVMT NNVAYGNGSS GLVVQRGLED LALPSNILID GGAYYDNARE GVLLKMTSDI TLQNADIHGN GSSGVRVYGA QDVQILDNQI HDNAQAAAVP EVLLQSFDDT AGASGTYYTT LNTRIEGNTI SGSANSTYGI QERNDGTDYS SLIDNDIAGV QQPIQLYGPH STVSGEPGAT PQQPSTGSDG EPLVGGDTDD QLQGGSGADR LDGGAGDDIL DGGAGRDRLS GGAGADTFVF SAREDSYRTD TAVFNDLILD FEASEDRIDL SALGFSGLGD GYGGTLLLKT NAEGTRTYLK SFEADAEGRR FEVALDGDHT GDLSAANVVF AATGTTTELE VLGDSGTQAG AIV //