ID ALGE2_AZOVI STANDARD; PRT; 997 AA. AC Q44495; 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 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, 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 C-5- RT epimerase gene."; RL J. Bacteriol. 176:2846-2853(1994). RN [2] 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 [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: Extracellular. Probably exported via the CC 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 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 11 hemolysin-type calcium-binding repeats. CC -!- SIMILARITY: Contains 7 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; AAA87312.1; -. DR PIR; S77625; S77625. DR InterPro; IPR006633; CASH. DR InterPro; IPR001343; Hemlysn_Ca_bind. DR InterPro; IPR006626; PbH1. DR InterPro; IPR011050; Pectin_lyas_like. DR InterPro; IPR003995; RtxA. DR InterPro; IPR011049; Serralysn_like_C. DR Pfam; PF00353; HemolysinCabind; 11. DR PRINTS; PR00313; CABNDNGRPT. DR PRINTS; PR01488; RTXTOXINA. DR SMART; SM00722; CASH; 2. DR SMART; SM00710; PbH1; 7. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6. KW Alginate biosynthesis; Calcium; Direct protein sequencing; Isomerase; KW 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 280 315 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 //