ID   MANI_PSEC1              Reviewed;         414 AA.
AC   A0A0P9JFY5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=D-mannose isomerase {ECO:0000303|PubMed:33484446};
DE            Short=PsMIaseA {ECO:0000303|PubMed:33484446};
DE            EC=5.3.1.7 {ECO:0000269|PubMed:33484446};
GN   ORFNames=ALO83_00665 {ECO:0000312|EMBL:KPW23544.1};
OS   Pseudomonas cannabina pv. alisalensis (strain ATCC BAA-566 / CFBP 6866 /
OS   ICMP 15200 / BS91).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1292044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-566 / CFBP 6866 / ICMP 15200 / BS91;
RA   Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT   "Genome announcement of multiple Pseudomonas syringae strains.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND BIOTECHNOLOGY.
RX   PubMed=33484446; DOI=10.1007/s12010-021-03487-y;
RA   Hua X., Li Y., Jiang Z., Ma J., Liu H., Yan Q.;
RT   "Biochemical properties of a novel D-mannose isomerase from Pseudomonas
RT   syringae for D-mannose production.";
RL   Appl. Biochem. Biotechnol. 193:1482-1495(2021).
CC   -!- FUNCTION: Catalyzes the reversible isomerization of D-mannose to D-
CC       fructose (PubMed:33484446). Shows high specific activity towards
CC       mannose and fructose, and has no detectable activity towards other
CC       monosaccharides and disaccharides (PubMed:33484446).
CC       {ECO:0000269|PubMed:33484446}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannose = D-fructose; Xref=Rhea:RHEA:22604,
CC         ChEBI:CHEBI:4208, ChEBI:CHEBI:37721; EC=5.3.1.7;
CC         Evidence={ECO:0000269|PubMed:33484446};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by Ag(2+), Cu(2+) and
CC       cetyltrimethyl ammonium bromide (CTAB). {ECO:0000269|PubMed:33484446}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=36.6 mM for mannose {ECO:0000269|PubMed:33484446};
CC         KM=175.5 mM for fructose {ECO:0000269|PubMed:33484446};
CC         Vmax=1044.6 umol/min/mg enzyme with mannose as substrate
CC         {ECO:0000269|PubMed:33484446};
CC         Vmax=792.6 umol/min/mg enzyme with fructose as substrate
CC         {ECO:0000269|PubMed:33484446};
CC         Note=kcat is 0.766 sec(-1) with mannose as substrate. kcat is 0.581
CC         sec(-1) with fructose as substrate. {ECO:0000269|PubMed:33484446};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:33484446};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Thermostable up to 45
CC         degrees Celsius. {ECO:0000269|PubMed:33484446};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:33484446}.
CC   -!- BIOTECHNOLOGY: Shows high production efficiency and may be suitable for
CC       green production of D-mannose. {ECO:0000269|PubMed:33484446}.
CC   -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; LJPP01000116; KPW23544.1; -; Genomic_DNA.
DR   RefSeq; WP_007249212.1; NZ_LJPP01000116.1.
DR   SMR; A0A0P9JFY5; -.
DR   EnsemblBacteria; KPW23544; KPW23544; ALO83_00665.
DR   EnsemblBacteria; RMN75583; RMN75583; ALQ52_02755.
DR   GeneID; 64465437; -.
DR   PATRIC; fig|663709.3.peg.1051; -.
DR   Proteomes; UP000050382; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Isomerase.
FT   CHAIN           1..414
FT                   /note="D-mannose isomerase"
FT                   /id="PRO_0000453302"
FT   ACT_SITE        255
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZKT7"
FT   ACT_SITE        390
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZKT7"
SQ   SEQUENCE   414 AA;  46083 MW;  701E82ABA88959DC CRC64;
     MDNNNHTFSS WLRSPAHHQW LALEGKRLLG FAKAAKLENG FGGLDDYGRL MVGATAGTMN
     TARMTHCFAM AHVQGIPGCA ALIDHGIAAL SGPLHDAEHG GWFSAALEDH GKTDKQAYLH
     AFVALAASSA VVAGRPAAQA LLSDVIQVIQ SRFWSDEEGA MRESFSQDWS DEEPYRGANS
     NMHSTEAFLA LADVTGDAQW LDRALSIVER VIHQHAGANN FQVIEHFTSG WQPLPDYNRE
     NPADGFRPFG TTPGHAFEWA RLVLHLEAAR RRAGRSNPDW LLDDARQLFA NACRYGWDVD
     GAPGIVYTLD WQNKPVVRHR LHWTHCEAAA AAAALLQRTG EQQYEDWYRC FWEFNETLFI
     DIEHGSWRHE LNERNEPSED IWPGKPDLYH AYQATLLPVL PLAPSLASAM AGLD