GenomeNet

Database: UniProt
Entry: R5G970_9FIRM
LinkDB: R5G970_9FIRM
Original site: R5G970_9FIRM 
ID   R5G970_9FIRM            Unreviewed;       355 AA.
AC   R5G970;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927, ECO:0000256|HAMAP-Rule:MF_00106};
DE            EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927, ECO:0000256|HAMAP-Rule:MF_00106};
DE   AltName: Full=D-mannonate hydro-lyase {ECO:0000256|HAMAP-Rule:MF_00106};
GN   Name=uxuA {ECO:0000256|HAMAP-Rule:MF_00106};
GN   ORFNames=BN498_01729 {ECO:0000313|EMBL:CCY13860.1};
OS   Eubacterium sp. CAG:146.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262879 {ECO:0000313|EMBL:CCY13860.1, ECO:0000313|Proteomes:UP000018404};
RN   [1] {ECO:0000313|EMBL:CCY13860.1, ECO:0000313|Proteomes:UP000018404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:146 {ECO:0000313|Proteomes:UP000018404};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dehydration of D-mannonate.
CC       {ECO:0000256|ARBA:ARBA00002713, ECO:0000256|HAMAP-Rule:MF_00106}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00106};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00106};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00106};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion. {ECO:0000256|ARBA:ARBA00004892, ECO:0000256|HAMAP-
CC       Rule:MF_00106}.
CC   -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC       {ECO:0000256|ARBA:ARBA00007389, ECO:0000256|HAMAP-Rule:MF_00106}.
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:CCY13860.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAXQ010000159; CCY13860.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5G970; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000018404; Unassembled WGS sequence.
DR   GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR   HAMAP; MF_00106; UxuA; 1.
DR   InterPro; IPR004628; Man_deHydtase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   NCBIfam; TIGR00695; uxuA; 1.
DR   PANTHER; PTHR30387; MANNONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR30387:SF2; MANNONATE DEHYDRATASE; 1.
DR   Pfam; PF03786; UxuA; 1.
DR   PIRSF; PIRSF016049; Man_dehyd; 2.
DR   SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00106};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00106};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018404}.
SQ   SEQUENCE   355 AA;  40367 MW;  373B76C72389058C CRC64;
     MKMTLRWYGS SFDTVTLKQI RQIPGVTGVI STLYDTSPGE VWSRSRIHAL KREIEQAGLS
     LMGIESVNVH DSIKIGDSDR DVYIDNYIET LKHLGEEDIH LICYNFMPVF DWTRTELARV
     RPDGSTVLAY SQKAVDALNP DEMFQSISSD TNGTVMPGWE PERLKNIHAL FEMYKDVDSE
     KLFSNLVYFL NRIMPVCETY NIDMAIHPDD PAWNVFGLPR IITDKEHLLR LMKTVDNPHN
     GVTFCTGSLG TNPENDLPNM IRSLKGRIHF AHIRNLKHNF PGDFEEAAHL SSDGSFDMYA
     IVKALYDIGF DGPIRPDHGR MIWDEKAMPG YGLYDRALGA AYLNGLWEAI EKSSK
//
DBGET integrated database retrieval system