ALGG_PSEAE
ID ALGG_PSEAE Reviewed; 543 AA.
AC Q51371;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Mannuronan C5-epimerase {ECO:0000303|PubMed:8144447};
DE EC=5.1.3.37 {ECO:0000269|PubMed:15968068, ECO:0000269|PubMed:16866359, ECO:0000269|PubMed:8144447};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase {ECO:0000305};
DE Flags: Precursor;
GN Name=algG {ECO:0000303|PubMed:8144447}; OrderedLocusNames=PA3545;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-49, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=FRD1;
RX PubMed=8144447; DOI=10.1128/jb.176.7.1821-1830.1994;
RA Franklin M.J., Chitnis C.E., Gacesa P., Sonesson A., White D.C.,
RA Ohman D.E.;
RT "Pseudomonas aeruginosa AlgG is a polymer level alginate C5-mannuronan
RT epimerase.";
RL J. Bacteriol. 176:1821-1830(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD1;
RX PubMed=8550492; DOI=10.1128/jb.178.3.625-632.1996;
RA Monday S.R., Schiller N.L.;
RT "Alginate synthesis in Pseudomonas aeruginosa: the role of AlgL (alginate
RT lyase) and AlgX.";
RL J. Bacteriol. 178:625-632(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP FUNCTION, PATHWAY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-272.
RC STRAIN=FRD1;
RX PubMed=12581364; DOI=10.1046/j.1365-2958.2003.03361.x;
RA Jain S., Franklin M.J., Ertesvaag H., Valla S., Ohman D.E.;
RT "The dual roles of AlgG in C-5-epimerization and secretion of alginate
RT polymers in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 47:1123-1133(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF ARG-316; ASP-324;
RP PRO-325; HIS-326; ASP-327; ASN-361; ASN-362; SER-364; TYR-365; GLU-366;
RP ASN-367; VAL-383 AND TYR-385.
RC STRAIN=FRD1;
RX PubMed=15968068; DOI=10.1128/jb.187.13.4573-4583.2005;
RA Douthit S.A., Dlakic M., Ohman D.E., Franklin M.J.;
RT "Epimerase active domain of Pseudomonas aeruginosa AlgG, a protein that
RT contains a right-handed beta-helix.";
RL J. Bacteriol. 187:4573-4583(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=16866359; DOI=10.1021/bi060748f;
RA Jerga A., Stanley M.D., Tipton P.A.;
RT "Chemical mechanism and specificity of the C5-mannuronan epimerase
RT reaction.";
RL Biochemistry 45:9138-9144(2006).
CC -!- FUNCTION: Catalyzes the epimerization of beta-D-mannuronate to alpha-L-
CC guluronate during the synthesis of the linear polysaccharide alginate
CC (PubMed:8144447, PubMed:15968068, PubMed:16866359). In addition, is
CC part of a periplasmic protein complex that protects alginate from
CC degradation by AlgL by channeling the newly formed alginate polymer
CC through a scaffold that transfers the alginate polymer through the
CC periplasmic space to the outer membrane secretin AlgE (PubMed:12581364,
CC PubMed:15968068). {ECO:0000269|PubMed:12581364,
CC ECO:0000269|PubMed:15968068, ECO:0000269|PubMed:16866359,
CC ECO:0000269|PubMed:8144447}.
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:15968068, ECO:0000269|PubMed:16866359,
CC ECO:0000269|PubMed:8144447};
CC -!- ACTIVITY REGULATION: Inhibited by the presence of acetyl groups on the
CC substrate. {ECO:0000269|PubMed:8144447}.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC {ECO:0000269|PubMed:12581364, ECO:0000269|PubMed:8144447}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8144447}.
CC -!- DOMAIN: The C-terminal region contains a right-handed beta-helix
CC (RHbetaH) fold, which is common among proteins that bind and cleave
CC long-chain linear polysaccharides. {ECO:0000269|PubMed:15968068}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant has a non-mucoid phenotype and
CC secretes uronic acids instead of polymerized alginate.
CC {ECO:0000269|PubMed:12581364}.
CC -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC {ECO:0000305}.
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DR EMBL; U27829; AAA91125.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06933.1; -; Genomic_DNA.
DR PIR; F83202; F83202.
DR RefSeq; NP_252235.1; NC_002516.2.
DR RefSeq; WP_003110465.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q51371; -.
DR SMR; Q51371; -.
DR STRING; 287.DR97_4397; -.
DR PaxDb; Q51371; -.
DR PRIDE; Q51371; -.
DR EnsemblBacteria; AAG06933; AAG06933; PA3545.
DR GeneID; 879839; -.
DR KEGG; pae:PA3545; -.
DR PATRIC; fig|208964.12.peg.3709; -.
DR PseudoCAP; PA3545; -.
DR HOGENOM; CLU_038044_0_0_6; -.
DR InParanoid; Q51371; -.
DR OMA; PHDRSHG; -.
DR PhylomeDB; Q51371; -.
DR BioCyc; MetaCyc:MON-19193; -.
DR BioCyc; PAER208964:G1FZ6-3613-MON; -.
DR BRENDA; 5.1.3.37; 5087.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002438; 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; IDA:PseudoCAP.
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; 7.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 1.
PE 1: Evidence at protein level;
KW Alginate biosynthesis; Direct protein sequencing; Isomerase; Periplasm;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:8144447"
FT CHAIN 36..543
FT /note="Mannuronan C5-epimerase"
FT /id="PRO_0000001125"
FT REPEAT 243..270
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 283..304
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 305..327
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 329..352
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 354..376
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 378..400
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT REPEAT 401..423
FT /note="PbH1 7"
FT /evidence="ECO:0000255"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q887Q3"
FT MUTAGEN 272
FT /note="S->N: Loss of epimerase activity; still capable of
FT protecting the polymer from depolymerization by AlgL
FT lyase."
FT /evidence="ECO:0000269|PubMed:12581364"
FT MUTAGEN 316
FT /note="R->A: Can complement the alginate secretion defect
FT and the epimerase defect of FRD1200 mutant, but cannot
FT complement the epimerase defect of FRD462 mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 324
FT /note="D->A: Can complement the alginate secretion defect
FT of FRD1200 mutant, but not the epimerization defect."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 325
FT /note="P->A: Can complement the alginate secretion defect
FT of FRD1200 mutant, but not the epimerization defect."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 326
FT /note="H->A: Can complement the alginate secretion defect
FT of FRD1200 mutant, but not the epimerization defect."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 327
FT /note="D->A: Can complement the alginate secretion defect
FT of FRD1200 mutant, but not the epimerization defect."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 361
FT /note="N->A: Can complement the alginate secretion defect
FT and the epimerase defect of FRD1200 mutant, but cannot
FT complement the epimerase defect of FRD462 mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 362
FT /note="N->A: Cannot complement the alginate secretion
FT defect of FRD1200 mutant or the epimerase defect of FRD462
FT mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 364
FT /note="S->A: Can complement the alginate secretion defect
FT of FRD1200 mutant and the epimerase defect of FRD462
FT mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 365
FT /note="Y->F: Can complement the alginate secretion defect
FT of FRD1200 mutant and the epimerase defect of FRD462
FT mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 366
FT /note="E->A: Can complement the alginate secretion defect
FT of FRD1200 mutant and the epimerase defect of FRD462
FT mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 367
FT /note="N->A: Cannot complement the alginate secretion
FT defect of FRD1200 mutant or the epimerase defect of FRD462
FT mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 383
FT /note="V->A: Cannot complement the alginate secretion
FT defect of FRD1200 mutant or the epimerase defect of FRD462
FT mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
FT MUTAGEN 385
FT /note="Y->F: Can complement the alginate secretion defect
FT of FRD1200 mutant and the epimerase defect of FRD462
FT mutant."
FT /evidence="ECO:0000269|PubMed:15968068"
SQ SEQUENCE 543 AA; 59802 MW; BCB1378EC4BB4192 CRC64;
MPDISLSIPR RRLPRLRPLA AAVLGAVLLH GQAWAAQPVE KPQPVPAQAG NEPGLTQGLK
ETGNYTVTTA PAEPLHLDPP KLPDLSGYTA AAVEAKIVRK PGGRASVQRM VQQQPLKEFT
GGSNRLAEWV KRQRQMPQAI FIEGGYVNLA QLAGKLPASA LEQVEPGVFV ARLPIVVSQG
ATLDIDKQVK ELRLSQERGA FLVNDGMLFV RDSKVTGWSE SKKEPAWFKT PNEFRPFLIS
WGGAEVYLSN STFTSFGYNA SKAYGISISQ YSPGMDKQMK RPRPKGWVID STIVDSWYGF
YCYEADDLVV KGNTYRDNIV YGIDPHDRSH RLIIADNTVH GTRKKHGIIV SREVNDSFIF
NNRSYENKLS GIVLDRNSEG NLVAYNEVYR NHSDGITLYE SGDNLLWGNQ VLANRRHGIR
VRNSVNIRLY ENLAAGNQLI GVYGHIKDLT NTDRNIALDP FDTKVSLIVV GGKLAGNGSG
PLSVDSPLSL ELYRVAMLAP TKSSGISLPG VLGEKQDQIL DLLVRQDKAV LIDPVESQAE
LQD
