ID   UXUA_CUTAK              Reviewed;         357 AA.
AC   Q6A5D2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Mannonate dehydratase {ECO:0000255|HAMAP-Rule:MF_00106};
DE            EC=4.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00106};
DE   AltName: Full=D-mannonate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00106};
GN   Name=uxuA {ECO:0000255|HAMAP-Rule:MF_00106}; OrderedLocusNames=PPA2327;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
CC   -!- FUNCTION: Catalyzes the dehydration of D-mannonate. {ECO:0000255|HAMAP-
CC       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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00106};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00106};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00106};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion. {ECO:0000255|HAMAP-Rule:MF_00106}.
CC   -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00106}.
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; AE017283; AAT84031.1; -; Genomic_DNA.
DR   RefSeq; WP_002515832.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A5D2; -.
DR   SMR; Q6A5D2; -.
DR   STRING; 267747.PPA2327; -.
DR   EnsemblBacteria; AAT84031; AAT84031; PPA2327.
DR   KEGG; pac:PPA2327; -.
DR   PATRIC; fig|267747.3.peg.2398; -.
DR   eggNOG; COG1312; Bacteria.
DR   HOGENOM; CLU_058621_1_0_11; -.
DR   OMA; GIVWALH; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000603; Chromosome.
DR   GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR   HAMAP; MF_00106; UxuA; 1.
DR   InterPro; IPR004628; Man_deHydtase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   PANTHER; PTHR30387; PTHR30387; 1.
DR   Pfam; PF03786; UxuA; 1.
DR   PIRSF; PIRSF016049; Man_dehyd; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR00695; uxuA; 1.
PE   3: Inferred from homology;
KW   Iron; Lyase; Manganese.
FT   CHAIN           1..357
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_0000170681"
SQ   SEQUENCE   357 AA;  40130 MW;  111AA2C65FFD26F4 CRC64;
     MKMTFRWYGA ETDPITLENI RQIPGVSGIM GAMDWIPVGE MWSDEEISSY VRKVNDAGLE
     CEVIESVNVH EDIKLGKPSR DIYIANYCKT LENLAAHGIK VVVYNFMPVF DWLRTELFHR
     NEDGSTCLYY DHEELVGLTP QDIVKATLDS SAFPLPGWEP ERLADLDEVM AQYTDMPRDQ
     LRNNYRYFLE GIVPTCEKVG IRMAVHPDDP AWGIFGIPRI VHSDSDLQRI VDLVNSPANS
     LCVCAGSLGS NPDNDVPAIL AKYGDMGRVA AAHVRNVKFL GSKKFKEASH LSSDGSLDMY
     AIMKSIHDHC SNSYIRPDHG RMIWGETGRP GYPLYDRALG ITYLNGLWEA IEKASAY