ID ALGE3_AZOVI Reviewed; 1839 AA.
AC Q44496;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Mannuronan C5-epimerase AlgE3 {ECO:0000305};
DE EC=5.1.3.37 {ECO:0000250|UniProtKB:Q44494};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase 3;
GN Name=algE3 {ECO:0000303|PubMed:7476166};
OS Azotobacter vinelandii.
OC Bacteria; Pseudomonadota; 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 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:0000250|UniProtKB:Q44494}.
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:0000250|UniProtKB:Q44494};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q44494};
CC -!- ACTIVITY REGULATION: Inhibited by zinc. {ECO:0000250|UniProtKB:Q44494}.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC {ECO:0000250|UniProtKB:Q44494}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Probably exported via the
CC 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 and
CC G-blocks, whereas the C-terminal A domain only generates MG-blocks.
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; AAA87313.1; -; Genomic_DNA.
DR PIR; S77626; S77626.
DR AlphaFoldDB; Q44496; -.
DR SMR; Q44496; -.
DR BRENDA; 5.1.3.37; 49.
DR UniPathway; UPA00286; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; Serralysin-like metalloprotease, C-terminal; 6.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF13229; Beta_helix; 2.
DR Pfam; PF00353; HemolysinCabind; 7.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR Pfam; PF08548; Peptidase_M10_C; 2.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00722; CASH; 4.
DR SMART; SM00710; PbH1; 16.
DR SUPFAM; SSF51120; beta-Roll; 7.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 11.
PE 3: Inferred from homology;
KW Alginate biosynthesis; Calcium; Isomerase; Repeat; Secreted.
FT CHAIN 1..1839
FT /note="Mannuronan C5-epimerase AlgE3"
FT /id="PRO_0000219557"
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..342
FT /note="PbH1 7"
FT /evidence="ECO:0000255"
FT REPEAT 347..369
FT /note="PbH1 8"
FT /evidence="ECO:0000255"
FT REPEAT 387..399
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 538..550
FT /note="Hemolysin-type calcium-binding 4"
FT /evidence="ECO:0000255"
FT REPEAT 557..573
FT /note="Hemolysin-type calcium-binding 5"
FT /evidence="ECO:0000255"
FT REPEAT 574..591
FT /note="Hemolysin-type calcium-binding 6"
FT /evidence="ECO:0000255"
FT REPEAT 695..709
FT /note="Hemolysin-type calcium-binding 7"
FT /evidence="ECO:0000255"
FT REPEAT 714..730
FT /note="Hemolysin-type calcium-binding 8"
FT /evidence="ECO:0000255"
FT REPEAT 732..748
FT /note="Hemolysin-type calcium-binding 9"
FT /evidence="ECO:0000255"
FT REPEAT 975..997
FT /note="PbH1 9"
FT /evidence="ECO:0000255"
FT REPEAT 999..1021
FT /note="PbH1 10"
FT /evidence="ECO:0000255"
FT REPEAT 1022..1044
FT /note="PbH1 11"
FT /evidence="ECO:0000255"
FT REPEAT 1046..1068
FT /note="PbH1 12"
FT /evidence="ECO:0000255"
FT REPEAT 1099..1121
FT /note="PbH1 13"
FT /evidence="ECO:0000255"
FT REPEAT 1122..1143
FT /note="PbH1 14"
FT /evidence="ECO:0000255"
FT REPEAT 1161..1183
FT /note="PbH1 15"
FT /evidence="ECO:0000255"
FT REPEAT 1188..1210
FT /note="PbH1 16"
FT /evidence="ECO:0000255"
FT REPEAT 1229..1243
FT /note="Hemolysin-type calcium-binding 10"
FT /evidence="ECO:0000255"
FT REPEAT 1247..1263
FT /note="Hemolysin-type calcium-binding 11"
FT /evidence="ECO:0000255"
FT REPEAT 1265..1281
FT /note="Hemolysin-type calcium-binding 12"
FT /evidence="ECO:0000255"
FT REPEAT 1398..1414
FT /note="Hemolysin-type calcium-binding 13"
FT /evidence="ECO:0000255"
FT REPEAT 1415..1432
FT /note="Hemolysin-type calcium-binding 14"
FT /evidence="ECO:0000255"
FT REPEAT 1536..1552
FT /note="Hemolysin-type calcium-binding 15"
FT /evidence="ECO:0000255"
FT REPEAT 1554..1571
FT /note="Hemolysin-type calcium-binding 16"
FT /evidence="ECO:0000255"
FT REPEAT 1670..1681
FT /note="Hemolysin-type calcium-binding 17"
FT /evidence="ECO:0000255"
FT REPEAT 1688..1704
FT /note="Hemolysin-type calcium-binding 18"
FT /evidence="ECO:0000255"
FT REPEAT 1706..1722
FT /note="Hemolysin-type calcium-binding 19"
FT /evidence="ECO:0000255"
FT REGION 372..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//
