ALGE1_AZOVI
ID ALGE1_AZOVI Reviewed; 1403 AA.
AC Q44494;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Mannuronan C5-epimerase AlgE1 {ECO:0000305};
DE EC=5.1.3.37 {ECO:0000269|PubMed:9812987};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase 1;
GN Name=algE1 {ECO:0000303|PubMed:7476166};
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 PubMed=7476166; DOI=10.1111/j.1365-2958.1995.tb02433.x;
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 alginate
RT structure in Azotobacter vinelandii.";
RL Mol. Microbiol. 16:719-731(1995).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND DOMAINS.
RC STRAIN=E;
RX PubMed=9812987; DOI=10.1074/jbc.273.47.30927;
RA Ertesvaag H., Hoeidal H.K., Skjaak-Braek G., Valla S.;
RT "The Azotobacter vinelandii mannuronan C-5-epimerase AlgE1 consists of two
RT separate catalytic domains.";
RL J. Biol. Chem. 273:30927-30932(1998).
RN [3]
RP DOMAINS.
RC STRAIN=E;
RX PubMed=10322003; DOI=10.1128/jb.181.10.3033-3038.1999;
RA Ertesvaag H., Valla S.;
RT "The A modules of the Azotobacter vinelandii mannuronan-C-5-epimerase AlgE1
RT are sufficient for both epimerization and binding of Ca2+.";
RL J. Bacteriol. 181:3033-3038(1999).
RN [4]
RP EXPRESSION.
RC STRAIN=E;
RX PubMed=11243259; 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 [5]
RP REVIEW.
RX PubMed=10937941; DOI=10.1006/mben.1999.0130;
RA Ertesvaag H., Hoeidal H.K., Schjerven H., Glaerum Svanem B.I., Valla S.;
RT "Mannuronan C-5-epimerases and their application for in vitro and in vivo
RT 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 acid
CC (G), producing a polymer with gel-forming capacity, required for the
CC formation of the cyst coat. {ECO:0000269|PubMed:9812987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-mannuronosyl](n) = [alginate](n);
CC Xref=Rhea:RHEA:45572, Rhea:RHEA-COMP:11264, Rhea:RHEA-COMP:11270,
CC ChEBI:CHEBI:58187, ChEBI:CHEBI:85311; EC=5.1.3.37;
CC Evidence={ECO:0000269|PubMed:9812987};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:9812987};
CC -!- ACTIVITY REGULATION: Inhibited by zinc. {ECO:0000269|PubMed:9812987}.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Probably exported via the
CC hemolysin-type secretion pathway.
CC -!- DEVELOPMENTAL STAGE: Produced during vegetative growth and in encysting
CC cells.
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 and
CC G- blocks, whereas the C-terminal A domain only generates MG-blocks.
CC {ECO:0000269|PubMed:10322003, ECO:0000269|PubMed:9812987}.
CC -!- MISCELLANEOUS: Each enzyme of this family of C5 epimerases introduces
CC its own characteristic sequence distribution of G-blocks in their
CC substrates, explaining the extensive sequence variability of alginates.
CC These alginates of varying composition have different physical
CC properties and are necessary at different stages of the bacterium life
CC cycle.
CC -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC {ECO:0000305}.
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DR EMBL; L39096; AAA87311.1; -; Genomic_DNA.
DR PIR; S77624; S77624.
DR AlphaFoldDB; Q44494; -.
DR SMR; Q44494; -.
DR BRENDA; 5.1.3.37; 49.
DR UniPathway; UPA00286; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.150.10.10; -; 3.
DR Gene3D; 2.160.20.10; -; 2.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF13229; Beta_helix; 2.
DR Pfam; PF00353; HemolysinCabind; 4.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SMART; SM00722; CASH; 4.
DR SMART; SM00710; PbH1; 15.
DR SUPFAM; SSF51120; SSF51120; 4.
DR SUPFAM; SSF51126; SSF51126; 2.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 9.
PE 1: Evidence at protein level;
KW Alginate biosynthesis; Calcium; Isomerase; Repeat; Secreted.
FT CHAIN 1..1403
FT /note="Mannuronan C5-epimerase AlgE1"
FT /id="PRO_0000219555"
FT REPEAT 133..155
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 157..179
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 180..202
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 204..226
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 257..279
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 280..302
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT REPEAT 320..359
FT /note="PbH1 7"
FT /evidence="ECO:0000255"
FT REPEAT 388..403
FT /note="Hemolysin-type calcium-binding 1"
FT /evidence="ECO:0000255"
FT REPEAT 406..422
FT /note="Hemolysin-type calcium-binding 2"
FT /evidence="ECO:0000255"
FT REPEAT 424..440
FT /note="Hemolysin-type calcium-binding 3"
FT /evidence="ECO:0000255"
FT REPEAT 557..573
FT /note="Hemolysin-type calcium-binding 4"
FT /evidence="ECO:0000255"
FT REPEAT 574..591
FT /note="Hemolysin-type calcium-binding 5"
FT /evidence="ECO:0000255"
FT REPEAT 697..712
FT /note="Hemolysin-type calcium-binding 6"
FT /evidence="ECO:0000255"
FT REPEAT 716..732
FT /note="Hemolysin-type calcium-binding 7"
FT /evidence="ECO:0000255"
FT REPEAT 734..750
FT /note="Hemolysin-type calcium-binding 8"
FT /evidence="ECO:0000255"
FT REPEAT 977..999
FT /note="PbH1 8"
FT /evidence="ECO:0000255"
FT REPEAT 1001..1023
FT /note="PbH1 9"
FT /evidence="ECO:0000255"
FT REPEAT 1024..1046
FT /note="PbH1 10"
FT /evidence="ECO:0000255"
FT REPEAT 1048..1070
FT /note="PbH1 11"
FT /evidence="ECO:0000255"
FT REPEAT 1101..1123
FT /note="PbH1 12"
FT /evidence="ECO:0000255"
FT REPEAT 1124..1146
FT /note="PbH1 13"
FT /evidence="ECO:0000255"
FT REPEAT 1163..1185
FT /note="PbH1 14"
FT /evidence="ECO:0000255"
FT REPEAT 1190..1212
FT /note="PbH1 15"
FT /evidence="ECO:0000255"
FT REPEAT 1227..1243
FT /note="Hemolysin-type calcium-binding 9"
FT /evidence="ECO:0000255"
FT REPEAT 1244..1261
FT /note="Hemolysin-type calcium-binding 10"
FT /evidence="ECO:0000255"
FT REPEAT 1263..1279
FT /note="Hemolysin-type calcium-binding 11"
FT /evidence="ECO:0000255"
FT REGION 372..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 147169 MW; 4E843AB0A366A95C CRC64;
MDYNVKDFGA LGDGVSDDTA AIQAAIDAAH AAGGGTVYLP AGEYRVSGGE EPSDGCLTIK
SNVHIVGAGM GETVIKMVDG WTQNVTGMVR SAYGEETSNF GMSDLTLDGN RDNLSAKVDG
WFNGYIPGQD GADRDVTLER VEIREMSGYG FDPHEQTINL TIRDSVAHDN SLDGFVADYQ
VGGVFENNVS YNNDRHGFNI VTSTNDFVLS NNVAYGNGGA GLVVQRGSYD LPHPYDILID
GGAYYDNALE GVQLKMAHDV TLQNAEIYGN GLYGVRVYGA QDVQILDNQI HDNSQNGAYA
EVLLQSYDDT AGVSGNFYVT TGTWLEGNVI SGSANSTYGI QERADGTDYS SLYANSIDGV
QTGAVRLYGA NSTVSSQSGS GQQATLEGSA GNDALSGTEA HETLLGQAGD DRLNGDAGND
ILDGGAGRDN LTGGAGADTF RFSARTDSYR TDSASFNDLI TDFDADEDSI DLSALGFTGL
GDGYNGTLLL KTNAEGTRTY LKSYEADAQG RRFEIALDGN FTGLFNDNNL LFDAAPATGT
EGSDNLLGTD AGETLLGYGG NDTLNGGAGD DILVGGAGRD SLTGGAGADV FRFDALSDSQ
RNYTTGDNQA DRILDFDPTL DRIDVSALGF TGLGNGRNGT LAVVLNSAGD RTDLKSYDTD
ANGYSFELSL AGNYQGQLSA EQFVFATSQG GQMTIIEGTD GNDTLQGTEA NERLLGLDGR
DNLNGGAGDD ILDGGAGRDT LTGGTGADTF LFSTRTDSYR TDSASFNDLI TDFDPTQDRI
DLSGLGFSGF GNGYDGTLLL QVNAAGTRTY LKSFEADANG QRFEIALDGD FSGQLDSGNV
IFEPAVFNAK DFGALGDGAS DDRPAIQAAI DAAYAAGGGT VYLPAGEYRV SPTGEPGDGC
LMLKDGVYLA GDGIGETVIK LIDGSDQKIT GMVRSAYGEE TSNFGMSDLT LDGNRDNTSG
KVDGWFNGYI PGQDGADRNV TIERVEIREM SGYGFDPHEQ TINLTIRDSV AHDNGLDGFV
ADYLVDSVFE NNVAYNNDRH GFNIVTSTYD FVMTNNVAYG NGGAGLTIQR GSEDLAQPTD
ILIDGGAYYD NALEGVLFKM TNNVTLQNAE IYGNGSSGVR LYGTEDVQIL DNQIHDNSQN
GTYPEVLLQA FDDSQVTGEL YETLNTRIEG NLIDASDNAN YAVRERDDGS DYTTLVDNDI
SGGQVASVQL SGAHSSLSGG TVEVPQGTDG NDVLVGSDAN DQLYGGAGDD RLDGGAGDDL
LDGGAGRDDL TGGTGADTFV FAARTDSYRT DAGVFNDLIL DFDASEDRID LSALGFSGFG
DGYNGTLLVQ LSSAGTRTYL KSYEEDLEGR RFEVALDGDH TGDLSAANVV FADDGSAAVA
SSDPAATQLE VVGSSGTQTD QLA
