ID   MANI_THEFU              Reviewed;         407 AA.
AC   A0A077LPS9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=D-mannose isomerase {ECO:0000303|Ref.1};
DE            EC=5.3.1.7 {ECO:0000269|Ref.1};
GN   Name=manI {ECO:0000303|Ref.1};
OS   Thermobifida fusca (Thermomonospora fusca).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=2021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=MBL10003;
RX   DOI=10.5458/jag.jag.JAG-2013_008;
RA   Kasumi T., Mori S., Kaneko S., Matsumoto H., Kobayashi Y., Koyama Y.;
RT   "Characterization of mannose isomerase from a cellulolytic actinobacteria
RT   Thermobifida fusca MBL10003.";
RL   J. Appl. Glycosci. 61:21-25(2014).
CC   -!- FUNCTION: Catalyzes the reversible isomerization of D-mannose to D-
CC       fructose. Shows weaker activity on D-lyxose, but cannot use N-acetyl D-
CC       glucosamine. {ECO:0000269|Ref.1}.
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|Ref.1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-lyxose = D-xylulose; Xref=Rhea:RHEA:14201,
CC         ChEBI:CHEBI:16789, ChEBI:CHEBI:17140; Evidence={ECO:0000269|Ref.1};
CC   -!- ACTIVITY REGULATION: Significantly inhibited by divalent metal ions
CC       such as Cu(2+), Cd(2+) or Ca(2+). {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=115 mM for D-mannose {ECO:0000269|Ref.1};
CC         KM=537 mM for D-lyxose {ECO:0000269|Ref.1};
CC         Note=kcat is 788 sec(-1) with D-mannose as substrate. kcat is 63.3
CC         sec(-1) with D-lyxose as substrate. {ECO:0000269|Ref.1};
CC       pH dependence:
CC         Optimum pH is around 8.0. Stable between pH 4 and 11.
CC         {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; AB761401; BAP46301.1; -; Genomic_DNA.
DR   SMR; A0A077LPS9; -.
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..407
FT                   /note="D-mannose isomerase"
FT                   /id="PRO_0000453303"
FT   ACT_SITE        251
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZKT7"
FT   ACT_SITE        383
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZKT7"
SQ   SEQUENCE   407 AA;  44917 MW;  720846E78388F78B CRC64;
     MTLWTARAAH RAWLDAEARR LVDFAAAADH PEHGFAWLDG SGAPLPEQGV HTWITCRVTH
     VAALAHLEGI PGASALADHG LRALAGPLRD PEHDGWFTAL DSRGTVADSR KEAYQHAFVL
     LAAASATVAG RPGARELLDA AAAVIEQRFW EEETGRCRES WDAAWHADEP YRGANSNMHL
     VEAFLAAFDA TGDRVWAERA LRIAHFFVHE VAAPRDWRLP EHFTPDWQVV ADYNTDDRAH
     PFRPYGVTVG HVLEWARLLV HVEAALPDPP SWLLADAEAM FAAAVARGWS VDGTEGFVYT
     LDYDDTPVVR SRMHWVVAEA ISAAAVLGQR TGDERYEHWY RTWWDHAATY FVDTVQGSWH
     HELDPTLAPP PGGTWSGKPD VYHAYQATRL PLLPLAPSLA GALATVG