ALGG_PSEFL
ID ALGG_PSEFL Reviewed; 529 AA.
AC P59828;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Mannuronan C5-epimerase {ECO:0000305};
DE EC=5.1.3.37 {ECO:0000269|PubMed:11707327};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase {ECO:0000250|UniProtKB:Q51371};
DE Flags: Precursor;
GN Name=algG {ECO:0000303|PubMed:11707327};
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF SER-337; ASP-361; ARG-408 AND GLY-430.
RC STRAIN=ATCC 17397 / DSM 50091 / CIP 73.25 / NCIMB 10525 / 12;
RX PubMed=12775688; DOI=10.1128/jb.185.12.3515-3523.2003;
RA Gimmestad M., Sletta H., Ertesvaag H., Bakkevig K., Jain S., Suh S.-J.,
RA Skjaak-Braek G., Ellingsen T.E., Ohman D.E., Valla S.;
RT "The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-
RT epimerase activity, is needed for alginate polymer formation.";
RL J. Bacteriol. 185:3515-3523(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=1586;
RX PubMed=11707327; DOI=10.1016/s0378-1119(01)00685-0;
RA Morea A., Mathee K., Franklin M.J., Giacomini A., O'Regan M., Ohman D.E.;
RT "Characterization of algG encoding C5-epimerase in the alginate
RT biosynthetic gene cluster of Pseudomonas fluorescens.";
RL Gene 278:107-114(2001).
CC -!- FUNCTION: Catalyzes the epimerization of beta-D-mannuronate to alpha-L-
CC guluronate during the synthesis of the linear polysaccharide alginate
CC (PubMed:11707327). In addition, is part of a periplasmic protein
CC complex that protects alginate from degradation by AlgL by channeling
CC the newly formed alginate polymer through a scaffold that transfers the
CC alginate polymer through the periplasmic space to the outer membrane
CC secretin AlgE (PubMed:12775688). {ECO:0000269|PubMed:11707327,
CC ECO:0000269|PubMed:12775688}.
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:11707327};
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q51371}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant has a non-mucoid phenotype
CC (PubMed:11707327, PubMed:12775688). Mutant produces predominantly an
CC unsaturated disaccharide originating from degradation by AlgL
CC (PubMed:12775688). {ECO:0000269|PubMed:11707327,
CC ECO:0000269|PubMed:12775688}.
CC -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC {ECO:0000305}.
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DR EMBL; AF527790; AAP46694.1; -; Genomic_DNA.
DR AlphaFoldDB; P59828; -.
DR SMR; P59828; -.
DR eggNOG; COG3420; Bacteria.
DR BRENDA; 5.1.3.37; 5121.
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; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR007742; NosD_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; PF05048; NosD; 1.
DR SMART; SM00722; CASH; 1.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 2.
PE 1: Evidence at protein level;
KW Alginate biosynthesis; Isomerase; Periplasm; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..529
FT /note="Mannuronan C5-epimerase"
FT /id="PRO_0000001126"
FT REPEAT 229..256
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 291..313
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 315..338
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 340..362
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 364..386
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 387..409
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q887Q3"
FT MUTAGEN 337
FT /note="S->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:12775688"
FT MUTAGEN 361
FT /note="D->N: Loss of function."
FT /evidence="ECO:0000269|PubMed:12775688"
FT MUTAGEN 408
FT /note="R->C: Loss of function."
FT /evidence="ECO:0000269|PubMed:12775688"
FT MUTAGEN 430
FT /note="G->D: Loss of function."
FT /evidence="ECO:0000269|PubMed:12775688"
SQ SEQUENCE 529 AA; 58203 MW; B17B4EDE0A8614B3 CRC64;
MGACAMNPQA LKGSAMLAAA MLLASGAAMA DVAPQAKAPT IAKELQQAKT YTISSPPTAP
LEMAKPALPA LSGYTDAAME KKIVRAKPGK ISIRRMMQED ALKDFIGGDN KMAEWVVRQH
GIPQAIFIDD GYMNLKDLLG KVPKQYLSET SPGVFLAKLP IVVGRKGILE IDKKTQELRL
SQEAGSFLIN DGQLFVRDTK VTGWSEKANG PALYKSPKEF RPFLLAWGGT ETYISNTKMA
SFGYANSKSY GVSISQYTPN MAKVLKRPEP TGWIIDSEFS DMWYGFYCYE TTGFVIKGNT
YKDNIVYGID PHDRSHGLII ADNTVYGTKK KHGIIISREV NDSFIFNNRS YDNKLSGLVL
DRNSVNNFVA DNEFYRNHTD GITLYESGDN LLWGNKVIAN RRHGIRVRNS VNIKLYENTS
MANGLTGLYG HIKDLTDTDR DIALDPFDAK VSLIVVGGEL AGNGSGPLSI DSPLSVELYR
VSMLAPTKSS GISFNGVLGD RQEEILDLLV RQQKAVLIDP VERQTELQD
