ALGG_PSEPK
ID ALGG_PSEPK Reviewed; 519 AA.
AC Q88NC9;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Mannuronan C5-epimerase {ECO:0000250|UniProtKB:Q51371};
DE EC=5.1.3.37 {ECO:0000250|UniProtKB:Q51371};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase {ECO:0000250|UniProtKB:Q51371};
DE Flags: Precursor;
GN Name=algG; OrderedLocusNames=PP_1283;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: Catalyzes the epimerization of beta-D-mannuronate to alpha-L-
CC guluronate during the synthesis of the linear polysaccharide alginate.
CC In addition, is part of a periplasmic protein complex that protects
CC alginate from degradation by AlgL by channeling the newly formed
CC alginate polymer through a scaffold that transfers the alginate polymer
CC through the periplasmic space to the outer membrane secretin AlgE.
CC {ECO:0000250|UniProtKB:Q51371}.
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:Q51371};
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC {ECO:0000250|UniProtKB:Q51371}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q51371}.
CC -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN66907.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015451; AAN66907.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_743443.2; NC_002947.4.
DR RefSeq; WP_003251754.1; NC_002947.4.
DR AlphaFoldDB; Q88NC9; -.
DR SMR; Q88NC9; -.
DR STRING; 160488.PP_1283; -.
DR EnsemblBacteria; AAN66907; AAN66907; PP_1283.
DR KEGG; ppu:PP_1283; -.
DR PATRIC; fig|160488.4.peg.1360; -.
DR eggNOG; COG3420; Bacteria.
DR HOGENOM; CLU_038044_0_0_6; -.
DR OMA; PHDRSHG; -.
DR PhylomeDB; Q88NC9; -.
DR BioCyc; PPUT160488:G1G01-1370-MON; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000000556; Chromosome.
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; 6.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 1.
PE 3: Inferred from homology;
KW Alginate biosynthesis; Isomerase; Periplasm; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..519
FT /note="Mannuronan C5-epimerase"
FT /id="PRO_0000001127"
FT REPEAT 219..246
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 281..303
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 305..328
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 330..352
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 354..376
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 377..399
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT ACT_SITE 302
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q887Q3"
SQ SEQUENCE 519 AA; 57936 MW; 804D0CA87D39EDCC CRC64;
MNLHPHLRHS LLASALLLAS GLATAAEPQV IAKELQQAKT YTVASAPIEP LQMDPPKLPD
LTGFTAEAVQ KKIDRRHKGK VSLRRMFQED TLKEFVGGDN KAAEWVQRQH GIPQAIFVDD
GHVDLTELSK KVPKQYFSEV EPGVYLARLP IVVGQKGILE IDGKVKQLRL SQEGGAFLVN
DGKLFVTDTQ VTGWREKDNG PATFRSPKEF RPFLLSWGGT ETYIVNTKMA SFGYAKSKSY
GVSISQYTPN MAKRMGRPEP TGWIIGSEFS DMWYGFYCYE TQDFVIKDST YRDNIVYGID
PHDRSHRLII AGNTVYGTKK KHGIIVSREV NDSWIINNKS YDNKLSGVVI DRNSVNNLVA
YNEIYRNHTD GITLYESGDN LIWGNKLVNN RRHGIRVRNS VNIRLYENVA MANGLVGVYG
HIKDLSDTDR DIALDPFDTK VSLIVVGGEL SANGSGPLSI DSPLSVELYK VSMLAPRKAS
GISLNGVLGE RQDEILDLLV RQQKAVLIDP VERQTEMID
