ID   ALGG_AZOVI              Reviewed;         525 AA.
AC   P70805;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Mannuronan C5-epimerase AlgG {ECO:0000303|PubMed:8830682};
DE            EC=5.1.3.37 {ECO:0000269|PubMed:8830682};
DE   AltName: Full=Poly(beta-D-mannuronate) C5 epimerase {ECO:0000250|UniProtKB:Q51371};
DE   Flags: Precursor;
GN   Name=algG {ECO:0000303|PubMed:8830682};
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND INDUCTION.
RC   STRAIN=E;
RX   PubMed=8830682; DOI=10.1128/jb.178.20.5884-5889.1996;
RA   Rehm B.H.A., Ertesvaag H., Valla S.;
RT   "A new Azotobacter vinelandii mannuronan C-5-epimerase gene (algG) is part
RT   of an alg gene cluster physically organized in a manner similar to that in
RT   Pseudomonas aeruginosa.";
RL   J. Bacteriol. 178:5884-5889(1996).
CC   -!- FUNCTION: Catalyzes the epimerization of beta-D-mannuronate to alpha-L-
CC       guluronate during the synthesis of the linear polysaccharide alginate
CC       (PubMed:8830682). In addition, is part of a periplasmic protein complex
CC       that protects alginate from degradation by AlgL by channeling the newly
CC       formed alginate polymer through a scaffold that transfers the alginate
CC       polymer through the periplasmic space to the outer membrane secretin
CC       AlgE (By similarity). {ECO:0000250|UniProtKB:Q51371,
CC       ECO:0000269|PubMed:8830682}.
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:8830682};
CC   -!- ACTIVITY REGULATION: Inhibited by zinc. {ECO:0000269|PubMed:8830682}.
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC       {ECO:0000250|UniProtKB:Q51371}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q51371}.
CC   -!- INDUCTION: Produced during vegetative growth.
CC       {ECO:0000269|PubMed:8830682}.
CC   -!- MISCELLANEOUS: This epimerase does not require calcium for its
CC       activity. Probably cannot form G blocks. {ECO:0000269|PubMed:8830682}.
CC   -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; X87973; CAA61231.1; -; Genomic_DNA.
DR   AlphaFoldDB; P70805; -.
DR   SMR; P70805; -.
DR   UniPathway; UPA00286; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR   InterPro; IPR022441; Para_beta_helix_rpt-2.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF13229; Beta_helix; 1.
DR   SMART; SM00722; CASH; 1.
DR   SMART; SM00710; PbH1; 5.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   TIGRFAMs; TIGR03804; para_beta_helix; 1.
PE   1: Evidence at protein level;
KW   Alginate biosynthesis; Isomerase; Periplasm; Repeat; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..525
FT                   /note="Mannuronan C5-epimerase AlgG"
FT                   /id="PRO_0000001124"
FT   REPEAT          287..309
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          311..334
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          336..358
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          360..382
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          383..405
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        308
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q887Q3"
SQ   SEQUENCE   525 AA;  58317 MW;  9F9DC15A318CDF3C CRC64;
     MNVQRKLAST QLKPVLLGVL LATSAWSQAA PPEQARQSAP PTLSSKQYSV TSASIEALKL
     DPPKLPDLSG YTHAAVEAKI RRKPGGRIAA AMLQQTALKD FTGGSGRLRE WIVRQGGMPH
     AIFIEGGYVE LGQLARQLPA NQFAETTPGV YVARVPIVVA PGATLHIGKN VKELRLSEER
     GAFLVNDGKL FITDTKLVGW SEKNNAPSAY RGPESFWAFL VSWGGTETYI SRRPVASLGY
     NTSKAYGVSI TQYTPEMHKR LKRPRPTGWL IDSVFEDIYY GFYCYEADDV VLKGNTYRDN
     IIYGIDPHDR SERLVIAENH VYGTKKKHGI IVSREVNNSW IINNRTHDNK LSGIVLDRNS
     EHNLVAYNEV YQNHSDGITL YESSNNLIWG NRLINNARHG IRMRNSVNIR IYENLSVVNQ
     LTGIYGHIKD LSSTDRDFKL DPFDTKVSMI VVGGQLTGNG SSPISVDSPL SLELYRVEML
     APTKSSGLTF TGILEDKQEE ILDLLVRRQK AVLIDPVVDL AQAEL