UXUA_MARMS
ID UXUA_MARMS Reviewed; 391 AA.
AC A6VZ12;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=Mmwyl1_2778;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000749; ABR71691.1; -; Genomic_DNA.
DR RefSeq; WP_012070467.1; NC_009654.1.
DR AlphaFoldDB; A6VZ12; -.
DR SMR; A6VZ12; -.
DR STRING; 400668.Mmwyl1_2778; -.
DR EnsemblBacteria; ABR71691; ABR71691; Mmwyl1_2778.
DR KEGG; mmw:Mmwyl1_2778; -.
DR eggNOG; COG1312; Bacteria.
DR HOGENOM; CLU_058621_2_0_6; -.
DR OMA; GIVWALH; -.
DR OrthoDB; 907794at2; -.
DR UniPathway; UPA00246; -.
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..391
FT /note="Mannonate dehydratase"
FT /id="PRO_1000075902"
SQ SEQUENCE 391 AA; 44006 MW; 54FF68FF2EED826E CRC64;
MEHTWRWFGP NDETTLTDIR QTGATGVVTA LHEIPNGEVW PVEAIKARKA MIEAHTLRWS
VVESVPVHED IKKRTGNYQE YIQNYKQTLL NLAECGIDTV CYNFMPVLDW TRTDLDYELP
DGSRALRFDQ TAFAAFELYI LERKGAESEY SDEEKAQAKI FLENLKAEDK DRLVANIIAG
LPGSEESYTI EQFREKLDEY AGIDKDKLRE HLKLFLEEIV PAAEQGGLRL AIHPDDPPRP
ILGLPRVVSV KDDIEWLLGA VPSPVNGITL CTGSYGVRAD NDLVDMVQRF GSNIFFTHLR
STKREEVAGS FHEASHLGGD VDMVGVVRAL LVEEKKRNDN NAPSLIPMRP DHGHQILNDL
EKNSKPGYSK LGRMKGLAEV RGLELGLKST L