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Database: UniProt
Entry: M0B508_NATA1
LinkDB: M0B508_NATA1
Original site: M0B508_NATA1 
ID   M0B508_NATA1            Unreviewed;       299 AA.
AC   M0B508;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE            EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
GN   ORFNames=C481_00150 {ECO:0000313|EMBL:ELZ05900.1};
OS   Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS   P-10747 / NBRC 102637 / 172P1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=29540 {ECO:0000313|EMBL:ELZ05900.1, ECO:0000313|Proteomes:UP000011554};
RN   [1] {ECO:0000313|EMBL:ELZ05900.1, ECO:0000313|Proteomes:UP000011554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12278 {ECO:0000313|EMBL:ELZ05900.1,
RC   ECO:0000313|Proteomes:UP000011554};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: Catalyzes the dehydration of D-mannonate.
CC       {ECO:0000256|ARBA:ARBA00002713}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC         Xref=Rhea:RHEA:20097, ChEBI:CHEBI:15377, ChEBI:CHEBI:17767,
CC         ChEBI:CHEBI:57990; EC=4.2.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001794};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion. {ECO:0000256|ARBA:ARBA00004892}.
CC   -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC       {ECO:0000256|ARBA:ARBA00007389}.
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:ELZ05900.1}.
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DR   EMBL; AOIO01000003; ELZ05900.1; -; Genomic_DNA.
DR   AlphaFoldDB; M0B508; -.
DR   STRING; 29540.C481_00150; -.
DR   PATRIC; fig|29540.5.peg.30; -.
DR   eggNOG; arCOG05324; Archaea.
DR   Proteomes; UP000011554; Unassembled WGS sequence.
DR   GO; GO:0008927; F:mannonate dehydratase activity; IEA:InterPro.
DR   GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR   InterPro; IPR004628; Man_deHydtase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   PANTHER; PTHR30387; MANNONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR30387:SF2; MANNONATE DEHYDRATASE; 1.
DR   Pfam; PF03786; UxuA; 2.
DR   SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011554}.
SQ   SEQUENCE   299 AA;  33657 MW;  2F14B039CF2E358F CRC64;
     MGVENAVVHT LEIGDGKTTW SYHDLLHLKN WYEDAGLDVN VIEGSVPLTD RVRLGMEGRD
     EDIEEFKEFI RHCGQLDIPV VCYDWMVGIR WARTEAHVEA RGGSLVTAYS NDRMHRGRAG
     PAIDASREQI WDALEYFLQE VTPVAEAAGV KLGLHPDDPP RESVGGVPRI INSPEAYQRV
     LDSYDSEHNG ITFCQGNFAA MGVDLPETIR RFGNRINFVH FRDVEGDADD FVETWHDEGP
     RDMLAAMEAY QDAVDDDVVM RPDHVPTMVG EDNSNPGYHT KGRLFAVGYM RGLLEQAQR
//
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