ID A0A0Q8AS04_9PSED Unreviewed; 529 AA.
AC A0A0Q8AS04;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=mannuronan 5-epimerase {ECO:0000256|ARBA:ARBA00012124};
DE EC=5.1.3.37 {ECO:0000256|ARBA:ARBA00012124};
DE AltName: Full=Poly(beta-D-mannuronate) C5 epimerase {ECO:0000256|ARBA:ARBA00044319};
GN ORFNames=ASD60_27760 {ECO:0000313|EMBL:KQZ84722.1};
OS Pseudomonas sp. Root562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736561 {ECO:0000313|EMBL:KQZ84722.1, ECO:0000313|Proteomes:UP000051426};
RN [1] {ECO:0000313|EMBL:KQZ84722.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ84722.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ84722.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ84722.1,
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:KQZ84722.1}.
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DR EMBL; LMGK01000016; KQZ84722.1; -; Genomic_DNA.
DR RefSeq; WP_056854502.1; NZ_LMGK01000016.1.
DR AlphaFoldDB; A0A0Q8AS04; -.
DR OrthoDB; 6189730at2; -.
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; 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 NCBIfam; NF038177; epimerase_AlgG; 1.
DR NCBIfam; TIGR03804; para_beta_helix; 1.
DR PANTHER; PTHR22990; F-BOX ONLY PROTEIN; 1.
DR PANTHER; PTHR22990:SF15; F-BOX ONLY PROTEIN 10; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR SMART; SM00722; CASH; 1.
DR SMART; SM00710; PbH1; 6.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..529
FT /note="mannuronan 5-epimerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006333858"
FT DOMAIN 248..408
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
SQ SEQUENCE 529 AA; 58373 MW; 20776296D0B46B20 CRC64;
MNHQARKGSI SLLAGAMLLA SATAFANVEP AAPLAGKQAT VAKELQQAKT YTVSSAPTAP
LELATPKLPD VSGYTAEAIA AKIVRGKAGK ISVRRMMQED ALKDFIGGDN KMAEWVVRQH
GIPQAIFVDD GYMNLKDLAK KLPKQYFSET SPGVFLARLP IVVGRNGILE IDKQTQELRL
SQEAGSFLVN DGKLFVRDTR ITGWREKDNG PATFKSPKEF RPFLLAWGGT ETYIANSKLA
SFGYANSKSY GVSISQYTPN MAKVLKRPEP TGWIVGSEFS DMWYGFYCYE TSNFVVKGNT
YKDNIVYGID PHDRSHGLII ADNTVYGTKK KHGIIISREV NDSFIFNNRS YDNKLSGLVI
DRNSVNNLIA YNEIYQNHTD GITLYESADN LLWGNKVVSN RRHGIRIRNS VNIRLYENIA
MANGLTGVYG HIKDLTNTDR DIKLDPFDAQ VSLIVVGGEL AANGSGPLSI DSPLSVELYR
VSMLAPTKSS GISFSGILGE RQDEILDLLV RQQKAVLIDP VERQTEMQD
//
