ID W4AJF1_9BACL Unreviewed; 355 AA.
AC W4AJF1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=C161_25855 {ECO:0000313|EMBL:ETT31459.1};
OS Paenibacillus sp. FSL R5-192.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT31459.1, ECO:0000313|Proteomes:UP000019041};
RN [1] {ECO:0000313|EMBL:ETT31459.1, ECO:0000313|Proteomes:UP000019041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT31459.1,
RC ECO:0000313|Proteomes:UP000019041};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT31459.1}.
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DR EMBL; ASPR01000049; ETT31459.1; -; Genomic_DNA.
DR RefSeq; WP_036673719.1; NZ_ASPR01000049.1.
DR AlphaFoldDB; W4AJF1; -.
DR GeneID; 83561066; -.
DR PATRIC; fig|1226754.4.peg.5232; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000019041; 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}.
SQ SEQUENCE 355 AA; 40810 MW; DA512A4531A2D96A CRC64;
MRMVFRWFGE GNDTVTLDHI RQIPGVEGIV WALHDVPAGE EWPMDKILAV KTAADKAGLH
LDVVESVNIH EDIKLGLPSR DKYIANYIKT MEKLAQVGVK VICYNFMPIF DWLRTDMHKE
MEDGSTALFY EHSKLADIEP LELVRRITEN SALTMPGWEP ERLQYLTGLF EAYKDVTEDH
MWEHARYFLQ EIMPTAERLG IRMAIHPDDP PWPIFGLPKI ITSQENVRKY LNLYDSPYNS
VTLCSGSLGA NADNDIIGMI HEFKDRIPFA HIRNVKIYDN GDFIETSHRS QDGSVDIAGV
VEAYHDIGYE GYARPDHGRH LWGEQCRPGY GLYDRALGIM YLWGVWDSLQ RRAKA
//