ID ALGE3_AZOVI STANDARD; PRT; 1839 AA. AC Q44496; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 21-MAR-2006, entry version 33. DE Poly(beta-D-mannuronate) C5 epimerase 3 (EC 5.1.3.-) (Mannuronan DE epimerase 3). GN Name=algE3; 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=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 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: Secreted protein; extracellular space. CC Probably exported via the hemolysin-type secretion pathway. 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 CC MG-blocks. 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 20 hemolysin-type calcium-binding repeats. CC -!- SIMILARITY: Contains 16 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; L39096; AAA87313.1; -; Genomic_DNA. DR PIR; S77626; S77626. 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; 20. DR PRINTS; PR00313; CABNDNGRPT. DR SMART; SM00722; CASH; 4. DR SMART; SM00710; PbH1; 2. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 11. KW Alginate biosynthesis; Calcium; Isomerase; Repeat. FT CHAIN 1 1839 Poly(beta-D-mannuronate) C5 epimerase 3. FT /FTId=PRO_0000219557. 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 320 342 PbH1 7. FT REPEAT 347 369 PbH1 8. 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 731 748 Hemolysin-type calcium-binding 9. FT REPEAT 975 997 PbH1 9. FT REPEAT 999 1021 PbH1 10. FT REPEAT 1022 1044 PbH1 11. FT REPEAT 1046 1068 PbH1 12. FT REPEAT 1099 1121 PbH1 13. FT REPEAT 1122 1143 PbH1 14. FT REPEAT 1161 1183 PbH1 15. FT REPEAT 1188 1210 PbH1 16. FT REPEAT 1228 1245 Hemolysin-type calcium-binding 10. FT REPEAT 1246 1263 Hemolysin-type calcium-binding 11. FT REPEAT 1264 1281 Hemolysin-type calcium-binding 12. FT REPEAT 1379 1396 Hemolysin-type calcium-binding 13. FT REPEAT 1397 1414 Hemolysin-type calcium-binding 14. FT REPEAT 1415 1432 Hemolysin-type calcium-binding 15. FT REPEAT 1536 1553 Hemolysin-type calcium-binding 16. FT REPEAT 1554 1571 Hemolysin-type calcium-binding 17. FT REPEAT 1669 1686 Hemolysin-type calcium-binding 18. FT REPEAT 1687 1704 Hemolysin-type calcium-binding 19. FT REPEAT 1705 1722 Hemolysin-type calcium-binding 20. SQ SEQUENCE 1839 AA; 191005 MW; 40C6E059B769CBA3 CRC64; MDFNVKDFGA LGDGASDDTA AIQAAIDAAH AAGGGTVYLP AGEYRVSGGE EPSDGALTIK SNVYIVGAGM GETVIKMVDG WTQNVTGMVR SAYGEETSNF GMSDLTLDGN RDNLSAKVDG WFNGYIPGQD GADRDVTLER VEIREMSGYG FDPHEQTINL TIRDSVAHDN GLDGFVADYQ VGGVFENNVS YNNDRHGFNI VTSTNDFVLS NNVAYGNGGA GLVVQRGSYD LPHPYDILID GGAYYDNALE GVQLKMTHDV TLQNAEIYGN GLYGVRVYGA QDVQLLDNQI HDNSQNGAYA EVLLQSYDDT AGVSGNFYVT TGTWLEGNVI SGSANSTFGI QERADGTDYS SLYANTIDGV QNGTVRLYGA NSTVSEQPSS GQQATLEGTA GNDVLSGTGA HELILGLAGN DRLDGGAGDD TLDGGAGRDT LTGGAGADTF RFSAREDSHR TDSASFTDLI TDFDASQDRI DLSALGFTGL GNGYDGTLAV TTGSGGTRTY LKSYEVDAQG RRFEIALDGN FVGQFNDGNL LFDAAPVTGT EGNDNLSGTD AGETLLGYGG NDTLNGGAGN DILVGGAGRD TLTGGAGADV FRFEALSDSQ RNYTAGDNQG DYIIDFAVGE DRIDVSALGY TGLGNGRNGT LAVVLNSAGD RTYVKSYDTD ANGYNFELSL AGNYQGLLGA EQFVFATPPE QATIEGTDGN DSLQGTGADE LLLGLGGRDS LNGGAGDDVL DGGAERDTLT GGTGADTFLF SARTDSYRTD SASFTDLITD FDPAQDRIDL SGLGFSGFGN GYDGTLLLQV NAAGTRTYLK SLEADADGQR FEIALDGDFS GQLDSGNVIF EAGVFNAKDF GALGDGASDD RPAIQAAIDA AYAAGGGTVY LPAGEYRVSP TGDPGDGCLM LKDGVYLVGA GMGETVIKLI DGSDQKITGM VRSAYGEETS NFGMSDLTLD GNRDNTSGKV DGWFNGYIPG QDGADRNVTL ERVEIREMSG YGFDPHEQTI NLTIRDSVAH DNGLDGFVAD YLVDSVFENN VAYNNDRHGF NVVTSTYDFT LSNNVAYGNG GAGLVIQRGA EDLAQPTDIL IDGGAYYDNA LEGVLLKMTN NITLQNAEIY GNGYSGVRLY GTEDVQILNN QIHDNAQNVA YAEVLLQSFN DVGVSGNFYA TTGTWIEGNV ISGSANSTYG IEERNDGTDY SSLYANTIDG VQTGAVRLNG AHSIVSDQPG TGQQATLEGT TGNDTLGGSD AHETLLGLDG DDRLDGGAGN DILDGGVGRD TLTGGAGADT FRFSAREDSY RTASTSFTDL ITDFDPAQDR IDLSALGFTG LGDGYDGTLL VTTGSGGSRT YLKSLEADAE GRRFEIALDG DFVGLLDASN LIFERPAIEG DAGDNALLGT SVAETLLGHA GNDTLDGAGG DDILVGGAGS DSLTGGAGAD VFRFDALSDS QRNYDTGDNQ GDRITDFAVG EDKLDVSALG FTGLGDGYNG TLVLVLNSAG DRTYVKSYEN GADGYRFEFS LDGNYQGLLG NEDFIFATPS GQQLLEGTAG NDSLQGTAAD EVIHGGSGRD TLAGGAGADV FRFSELTDSY RTDSASYADL ITDFDASEDR IDLSGLGFSG LGNGYGGTLA LQVNSAGTRT YLKSYEANAA GERFELSLDG DLSGLDESHL VFDERVVLAG GDGNDTLSGG SAAEELLGGA GNDSLSGGAG NDILDGGAGR DTLSGGSGSD IFRFGDALDS FRNYNSGANV TDSIADFTHG ADLIDLSALG YTGLGDGYNG TLAIVLNDAG TKTYLKDRGG DAEGNRFEIA LEGNHADQLD ASDFIFATAA AATGIEVVGS TPAEEQPVV //