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Database: UniProt
Entry: A0A0M9EJW4_9RHOB
LinkDB: A0A0M9EJW4_9RHOB
Original site: A0A0M9EJW4_9RHOB 
ID   A0A0M9EJW4_9RHOB        Unreviewed;       403 AA.
AC   A0A0M9EJW4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ECO:0000313|EMBL:KPA23216.1};
GN   ORFNames=shim_15120 {ECO:0000313|EMBL:KPA23216.1};
OS   Shimia sp. SK013.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA23216.1, ECO:0000313|Proteomes:UP000037951};
RN   [1] {ECO:0000313|EMBL:KPA23216.1, ECO:0000313|Proteomes:UP000037951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK013 {ECO:0000313|EMBL:KPA23216.1,
RC   ECO:0000313|Proteomes:UP000037951};
RA   Voget S., Kanukollu S., Daniel R., Engelen B.;
RT   "Genome Sequence of Shimia sp. SK013.";
RL   Submitted (MAR-2015) 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:KPA23216.1}.
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DR   EMBL; LAJH01000009; KPA23216.1; -; Genomic_DNA.
DR   RefSeq; WP_054001908.1; NZ_LAJH01000009.1.
DR   AlphaFoldDB; A0A0M9EJW4; -.
DR   STRING; 1389006.shim_15120; -.
DR   PATRIC; fig|1389006.3.peg.1546; -.
DR   OrthoDB; 9780250at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000037951; 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; 1.
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:UP000037951}.
SQ   SEQUENCE   403 AA;  44473 MW;  D27348B2506076D6 CRC64;
     MKQTWRWFGP ADTINVKDLP QIEVEGIVTS LHHIPPGAVW TVPEIRKRQA EIATPNGQET
     GLSWEVVESL PVSETLKTQG ADYADHIACY KESLRNLAAS GLRTVCYNFM PVLDWTRTNL
     AAKMAHGGTA MSFDVIDFAI FDLFLLKRAA ARDEYAAVTL SIAETRFAAM DDAAKKSLQN
     NIVAGLPGAN DNWTVTEVAA LLDTYRDIDS TKLRRNLIDF LSQVVPLAEE LGMRMCCHPD
     DPPFPLLGMP RVMSSVKDYE TVIGSIDSIA NGATLCTGSL GVDPNFDGPD FVRRLGHRIH
     FAHLRNTTRL APTDGDKTSF YEAMHLEGDT DMVGTIRALL AEETRRKSEG RTDCQIPMRP
     DHGQDILHDL NTDSMPGYPL IGRAKGLAEL RGIIATLSHL QQT
//
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