MANI_MARM1
ID MANI_MARM1 Reviewed; 394 AA.
AC F2JVT6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=D-mannose isomerase {ECO:0000303|PubMed:29107017};
DE Short=MI {ECO:0000303|PubMed:29107017};
DE EC=5.3.1.7 {ECO:0000269|PubMed:29107017};
GN OrderedLocusNames=Marme_2490 {ECO:0000312|EMBL:ADZ91722.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
RN [2] {ECO:0007744|PDB:5X32}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX PubMed=29107017; DOI=10.1016/j.biochi.2017.10.016;
RA Saburi W., Jaito N., Kato K., Tanaka Y., Yao M., Mori H.;
RT "Biochemical and structural characterization of Marinomonas mediterranead-
RT mannose isomerase Marme_2490 phylogenetically distant from known enzymes.";
RL Biochimie 144:63-73(2018).
CC -!- FUNCTION: Catalyzes the reversible isomerization of D-mannose to D-
CC fructose. Can also isomerize D-lyxose, with lower efficiency. In longer
CC reaction with a higher concentration of enzyme, it can isomerize 4-OH
CC D-mannose derivatives (D-talose and 4-O-monosaccharyl-D-mannose).
CC Cannot use D-glucose. {ECO:0000269|PubMed:29107017}.
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:29107017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-lyxose = D-xylulose; Xref=Rhea:RHEA:14201,
CC ChEBI:CHEBI:16789, ChEBI:CHEBI:17140;
CC Evidence={ECO:0000269|PubMed:29107017};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.7 mM for D-mannose {ECO:0000269|PubMed:29107017};
CC KM=42.3 mM for D-lyxose {ECO:0000269|PubMed:29107017};
CC KM=27.8 mM for D-talose {ECO:0000269|PubMed:29107017};
CC Note=kcat is 329 sec(-1) with D-mannose as substrate. kcat is 64.4
CC sec(-1) with D-lyxose as substrate. kcat is 0.319 sec(-1) with D-
CC talose as substrate. {ECO:0000269|PubMed:29107017};
CC pH dependence:
CC Optimum pH is 7.3 with D-mannose as substrate.
CC {ECO:0000269|PubMed:29107017};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius with D-mannose as
CC substrate. {ECO:0000269|PubMed:29107017};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29107017}.
CC -!- DOMAIN: The alpha7-alpha8 and alpha11-alpha12 loops of the catalytic
CC domain may participate in the formation of an open substrate-binding
CC site to provide sufficient space to bind 4-OH D-mannose derivatives.
CC {ECO:0000269|PubMed:29107017}.
CC -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC {ECO:0000305}.
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DR EMBL; CP002583; ADZ91722.1; -; Genomic_DNA.
DR RefSeq; WP_013661626.1; NC_015276.1.
DR PDB; 5X32; X-ray; 2.59 A; A/B=1-394.
DR PDBsum; 5X32; -.
DR SMR; F2JVT6; -.
DR STRING; 717774.Marme_2490; -.
DR EnsemblBacteria; ADZ91722; ADZ91722; Marme_2490.
DR KEGG; mme:Marme_2490; -.
DR PATRIC; fig|717774.3.peg.2575; -.
DR eggNOG; COG2942; Bacteria.
DR HOGENOM; CLU_042253_1_0_6; -.
DR OMA; WVQAETF; -.
DR OrthoDB; 783590at2; -.
DR Proteomes; UP000001062; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00249; AGE; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR034116; AGE_dom.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..394
FT /note="D-mannose isomerase"
FT /id="PRO_0000453301"
FT ACT_SITE 251
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKT7"
FT ACT_SITE 380
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKT7"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:5X32"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 72..88
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:5X32"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 173..190
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 249..265
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 271..286
FT /evidence="ECO:0007829|PDB:5X32"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 331..347
FT /evidence="ECO:0007829|PDB:5X32"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:5X32"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5X32"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:5X32"
SQ SEQUENCE 394 AA; 46113 MW; 586A2438CF7E86B7 CRC64;
MSYPAFDSKT FLEAHIEKTM AFYFPTCIDP EGGFFQFFKD DGSVYDPNTR HLVSSTRFIF
NFAQAYLHTN IAEYKHAAVH GIQYLRQRHQ SQSGGYVWLL DGGTNLDETN HCYGLAFVIL
AYSNALQIGL SEAEVWIEVT YDLLETHFWE NKHGLYLDEI SSDWKTVSPY RGQNANMHMC
EALMSAFDAT QNPKYLDRAK LLAKNICQKQ ASLSNSNEVW EHYTNDWQID WDYNKNDPKH
LFRPWGFQPG HQTEWAKLLL MLDKRSPENW YLPKAKYLFD LAYKKAWDTK KGGLHYGYAP
DGTVCDPDKY FWVQAESFAA AWLLYKATKD ETYYKQYLTL WEFSWNHMID HTFGAWYRIL
DENNAQYDNN KSPAGKTDYH TMGACYEVLK TLTL
