ID A0A0Q8ACF5_9PSED Unreviewed; 340 AA.
AC A0A0Q8ACF5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=mannuronan 5-epimerase {ECO:0000256|ARBA:ARBA00012124};
DE EC=5.1.3.37 {ECO:0000256|ARBA:ARBA00012124};
GN ORFNames=ASD60_16315 {ECO:0000313|EMBL:KQZ78511.1};
OS Pseudomonas sp. Root562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736561 {ECO:0000313|EMBL:KQZ78511.1, ECO:0000313|Proteomes:UP000051426};
RN [1] {ECO:0000313|EMBL:KQZ78511.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ78511.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ78511.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ78511.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQZ78511.1}.
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DR EMBL; LMGK01000025; KQZ78511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8ACF5; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000051426; 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 Pfam; PF13229; Beta_helix; 2.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Alginate biosynthesis {ECO:0000256|ARBA:ARBA00022841};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT DOMAIN 121..234
FT /note="Right handed beta helix"
FT /evidence="ECO:0000259|Pfam:PF13229"
FT DOMAIN 243..302
FT /note="Right handed beta helix"
FT /evidence="ECO:0000259|Pfam:PF13229"
SQ SEQUENCE 340 AA; 36981 MW; 9882B000BB91E7A5 CRC64;
MRGVSVLVSE LEVQNDIDGG NIIRLNGGAL TLKNNRVKID VAFDPSFTVS EIPWGQRPRF
WFVGLSDIAK KKRRSVLFNI VDNEFESSQL YAAGAIKLST RKKDELLRVS ELDNVFVRGG
ILRNRFVGFH GGIFINGGNK VLISDNVLMK NSYLAIIAGG KNIQITNNRI LYPGNGTTGD
GITVYDVMID GRISGNLIYA GSCYGIWVLA NHVNGLDIQR NTILNGITSG IYMSAKDVGG
YIGNVLVKYN VITGNAGFAV AVENGQDVAI SNNHFEGNAA GFSAQLYVSK LAKNITVKGN
TAAKKITPEW AKDMALYRHQ TYEDNEVFTP AINAQSVPSP
//
