ID A0A0D6T1Q6_9PSED Unreviewed; 413 AA.
AC A0A0D6T1Q6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=mannuronan 5-epimerase {ECO:0000256|ARBA:ARBA00012124};
DE EC=5.1.3.37 {ECO:0000256|ARBA:ARBA00012124};
GN ORFNames=SZ55_0655 {ECO:0000313|EMBL:KIV74518.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV74518.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV74518.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV74518.1,
RC ECO:0000313|Proteomes:UP000032531};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001550};
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005182}.
CC -!- SIMILARITY: Belongs to the D-mannuronate C5-epimerase family.
CC {ECO:0000256|ARBA:ARBA00010085}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIV74518.1}.
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DR EMBL; JYFT01000008; KIV74518.1; -; Genomic_DNA.
DR RefSeq; WP_044401217.1; NZ_JYFT01000008.1.
DR AlphaFoldDB; A0A0D6T1Q6; -.
DR PATRIC; fig|1604022.3.peg.5316; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000032531; Unassembled WGS sequence.
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; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR022442; SO_2930-like_dom.
DR NCBIfam; TIGR03805; beta_helix_1; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR SMART; SM00710; PbH1; 7.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Alginate biosynthesis {ECO:0000256|ARBA:ARBA00022841};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..413
FT /note="mannuronan 5-epimerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002313565"
FT DOMAIN 67..215
FT /note="Right handed beta helix"
FT /evidence="ECO:0000259|Pfam:PF13229"
SQ SEQUENCE 413 AA; 43776 MW; 788F2BB298D41302 CRC64;
MRIAPLSLLA LSLVLAACGE QDKAPTTHAD FQKDLQARLI KAKPGTVIEI PAGTYQLDRS
LSLKVSGVTL KGAGMDKTIL NFKGQKAGAE GLLVDASDFT IEDLALEDTK GDALKVVGGK
NIVIRNVRTE WTNGPATENG AYGIYPVQTE NTLIEGAVAI GASDAGIYVG QSRNVVVRNS
RAERNVAGIE IENTIGADVY DNIATGNTGG ILVFNMPNLQ QPGHGTRVYR NQVKDNDHDN
FGHKGTPVAS VPAGSGVVIN SNDDVEIFDN DIGGHRTANV IVSSYFSTGY TNLSTSESFD
PYPERIYIHG NRFGPGGDSP DNLELKALKL AKFGLNGRLP DILWDGYVNP AKLVDGKLPA
ELGICVDNGE ATLINVDGPN GYKNISTDMS AHRCTLPRLP EIVLGTPAKA PGA
//
