ALGG_PSESM
ID ALGG_PSESM Reviewed; 536 AA.
AC Q887Q3;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Mannuronan C5-epimerase {ECO:0000305};
DE EC=5.1.3.37 {ECO:0000269|PubMed:24398681};
DE AltName: Full=Alginate epimerase {ECO:0000303|PubMed:24398681};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase {ECO:0000250|UniProtKB:Q51371};
DE Flags: Precursor;
GN Name=algG; OrderedLocusNames=PSPTO_1238;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
RN [2] {ECO:0007744|PDB:4NK6, ECO:0007744|PDB:4NK8}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 46-536 OF WILD-TYPE AND MUTANT
RP ALA-317, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF
RP TYR-294; TYR-296; TYR-314; ASP-317; HIS-319; ASP-320; LYS-338; HIS-339;
RP SER-344; ARG-345; ASP-368; ARG-369; TYR-392; ARG-415 AND ASP-452.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=24398681; DOI=10.1074/jbc.m113.533158;
RA Wolfram F., Kitova E.N., Robinson H., Walvoort M.T., Codee J.D.,
RA Klassen J.S., Howell P.L.;
RT "Catalytic mechanism and mode of action of the periplasmic alginate
RT epimerase AlgG.";
RL J. Biol. Chem. 289:6006-6019(2014).
RN [3] {ECO:0007744|PDB:4OZY}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 69-491 OF MUTANT ASN-265.
RA Howell P.L., Wolfram F., Robinson H.;
RT "Crystal Structure of the periplasmic alginate epimerase AlgG T265N
RT mutant.";
RL Submitted (FEB-2014) to the PDB data bank.
RN [4] {ECO:0007744|PDB:4OZZ}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 69-492 OF MUTANT ASN-265/MET-268.
RA Howell P.L., Wolfram F., Robinson H.;
RT "Crystal Structure of the periplasmic alginate epimerase AlgG T265N T268M
RT double mutant.";
RL Submitted (FEB-2014) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the epimerization of beta-D-mannuronate to alpha-L-
CC guluronate during the synthesis of the linear polysaccharide alginate
CC (PubMed:24398681). 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 (By similarity). {ECO:0000250|UniProtKB:Q51371,
CC ECO:0000269|PubMed:24398681}.
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:24398681};
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC {ECO:0000250|UniProtKB:Q51371}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q51371}.
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:24398681}.
CC -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016853; AAO54763.1; -; Genomic_DNA.
DR RefSeq; NP_791068.1; NC_004578.1.
DR RefSeq; WP_011103483.1; NC_004578.1.
DR PDB; 4NK6; X-ray; 2.10 A; A=46-536.
DR PDB; 4NK8; X-ray; 2.29 A; A=46-536.
DR PDB; 4OZY; X-ray; 2.90 A; A=69-491.
DR PDB; 4OZZ; X-ray; 2.90 A; A=69-492.
DR PDBsum; 4NK6; -.
DR PDBsum; 4NK8; -.
DR PDBsum; 4OZY; -.
DR PDBsum; 4OZZ; -.
DR AlphaFoldDB; Q887Q3; -.
DR SMR; Q887Q3; -.
DR STRING; 223283.PSPTO_1238; -.
DR EnsemblBacteria; AAO54763; AAO54763; PSPTO_1238.
DR GeneID; 1182874; -.
DR KEGG; pst:PSPTO_1238; -.
DR PATRIC; fig|223283.9.peg.1259; -.
DR eggNOG; COG3420; Bacteria.
DR HOGENOM; CLU_038044_0_0_6; -.
DR OMA; PHDRSHG; -.
DR OrthoDB; 218034at2; -.
DR PhylomeDB; Q887Q3; -.
DR BRENDA; 5.1.3.37; 10904.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002515; 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; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alginate biosynthesis; Isomerase; Periplasm;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..536
FT /note="Mannuronan C5-epimerase"
FT /id="PRO_0000001128"
FT REPEAT 298..320
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 322..345
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 347..369
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 371..393
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 394..416
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:24398681"
FT MUTAGEN 294
FT /note="Y->A: Retains 24% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 294
FT /note="Y->F: Retains 66% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 296
FT /note="Y->A: Retains 66% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 314
FT /note="Y->F: Retains 5% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 317
FT /note="D->A: Retains 5% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 319
FT /note="H->A: Loss of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 320
FT /note="D->A: Loss of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 338
FT /note="K->A: Retains 87% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 339
FT /note="H->A: Retains 49% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 344
FT /note="S->A: Retains 54% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 345
FT /note="R->A,Q: Retains 10% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 345
FT /note="R->E: Loss of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 345
FT /note="R->K: Retains 36% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 368
FT /note="D->N: Retains 5% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 369
FT /note="R->A: Retains 23% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 392
FT /note="Y->F,A: Retains 65% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 415
FT /note="R->C: Loss of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT MUTAGEN 452
FT /note="D->A: Retains 63% of epimerase activity."
FT /evidence="ECO:0000269|PubMed:24398681"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:4NK6"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4NK6"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:4NK6"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4NK8"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:4NK6"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:4NK6"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 200..212
FT /evidence="ECO:0007829|PDB:4NK6"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 238..248
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4NK6"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4OZY"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:4NK6"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 459..469
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 471..477
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:4NK6"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:4OZZ"
SQ SEQUENCE 536 AA; 59486 MW; B17F41A67C6AA854 CRC64;
MNSHASNGRS RNWPHALLES ALLTSALLMA SSVALANAPA VPEAPKALVK ELHQAKTYTI
TSPPTGPLEM AKPVLPDLSG YTTEAALKKI ARNKPGKITV ARMMEETGLK EFIGGDNKMA
EWVVRQKGIP QAIMISDGYV NLQDLVKKVP KQFLSEVSPG VYVARLPILV KETGIFEIDS
KTKELRLSQE KGSFIVSEGK MLITNTSVNA WSETRNGLAA YRTPDEFRPF VLTWGGSQTW
IAKTKMASMG YNQSKSYGVS ISQYTPNTAK VLKRGEPTGW IIDSEFADMW YGFYCYETRD
FVVKGNTYRD NIVYGIDPHD RSHGLIIAEN DVYGTKKKHG IIISREVDNS FIFRNKSHNN
KLSGVVLDRN SVGNIVAYNE IYQNHTDGIT LYESGNNLLW GNRVIANRRH GIRVRNSVNI
KLYENVAMAN GLMGVYGHIK DLNDTDRDIE LDPFDAQVSL IMVGGELSSN GSGPLSIDSP
LSVELYRVSM LMPTKEVGIS LNGILGERQD EILDLLVRQK KAVLIDPVES QTELRE
