ID A0A1G3E1I0_9GAMM Unreviewed; 426 AA.
AC A0A1G3E1I0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=mannuronan 5-epimerase {ECO:0000256|ARBA:ARBA00012124};
DE EC=5.1.3.37 {ECO:0000256|ARBA:ARBA00012124};
DE Flags: Fragment;
GN ORFNames=A2Y50_10815 {ECO:0000313|EMBL:OHC25795.1};
OS Pseudomonadales bacterium RIFCSPLOWO2_12_59_9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales.
OX NCBI_TaxID=1802009 {ECO:0000313|EMBL:OHC25795.1, ECO:0000313|Proteomes:UP000179365};
RN [1] {ECO:0000313|EMBL:OHC25795.1, ECO:0000313|Proteomes:UP000179365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHC25795.1}.
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DR EMBL; MHZN01000289; OHC25795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3E1I0; -.
DR STRING; 1802009.A2Y50_10815; -.
DR Proteomes; UP000179365; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR039448; Beta_helix.
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 Pfam; PF13229; Beta_helix; 1.
DR SMART; SM00710; PbH1; 7.
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 217..331
FT /note="Right handed beta helix"
FT /evidence="ECO:0000259|Pfam:PF13229"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OHC25795.1"
SQ SEQUENCE 426 AA; 47685 MW; 69606028841F4D19 CRC64;
EFTGGDERLR EWVKRQGEVP QAIFIEGGYV TPADLARSLP PQYFRETAPG IYLARLPIVV
SQGATLHIGQ QTKDFRLSSE RGAFLINDGT LFITDTRLTA WRETENQQDW FKTKGEFRPF
LNAWGGTETY IVNSQVASLG YSGTKSYGVS ISQYSPGIAP TMGRGHPTGW LINSVFDDMW
YGFYCYEADD VVLKGNIYKN NIIYGIDPHD RSRRLIIAEN TVYGTHKKHG IIISRDVNDS
WIFNNRSFEN NLSGLVLDRL SVNNVLAGNE LYRNKSDGIT LYESGNNLLW GNKSFENARH
GIRVRNSMNV RLYENLAVAN GLLGIYGHTK DLNNIGRNLK QDPFSTDMSL TVVGGRLIAN
RTGDISVVAP RSVTLYRLDI LLPNQPSGIG MFGALSSHKN QIIDLLVRQQ KAVQILPVDQ
LTQSGQ
//
