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Database: UniProt
Entry: S2SFK7_LACPA
LinkDB: S2SFK7_LACPA
Original site: S2SFK7_LACPA 
ID   S2SFK7_LACPA            Unreviewed;       343 AA.
AC   S2SFK7;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE            EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
DE   Flags: Fragment;
GN   ORFNames=Lpp126_06690 {ECO:0000313|EMBL:EPC78253.1};
OS   Lacticaseibacillus paracasei subsp. paracasei Lpp126.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1256206 {ECO:0000313|EMBL:EPC78253.1, ECO:0000313|Proteomes:UP000014243};
RN   [1] {ECO:0000313|EMBL:EPC78253.1, ECO:0000313|Proteomes:UP000014243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lpp126 {ECO:0000313|EMBL:EPC78253.1,
RC   ECO:0000313|Proteomes:UP000014243};
RX   PubMed=23894338;
RA   Smokvina T., Wels M., Polka J., Chervaux C., Brisse S., Boekhorst J.,
RA   van Hylckama Vlieg J.E., Siezen R.J.;
RT   "Lactobacillus paracasei comparative genomics: towards species pan-genome
RT   definition and exploitation of diversity.";
RL   PLoS ONE 8:E68731-E68731(2013).
CC   -!- FUNCTION: Catalyzes the dehydration of D-mannonate.
CC       {ECO:0000256|ARBA:ARBA00002713}.
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};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion. {ECO:0000256|ARBA:ARBA00004892}.
CC   -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC       {ECO:0000256|ARBA:ARBA00007389}.
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:EPC78253.1}.
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DR   EMBL; ANKC01000473; EPC78253.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2SFK7; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000014243; Unassembled WGS sequence.
DR   GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-EC.
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   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};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EPC78253.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211}.
FT   NON_TER         343
FT                   /evidence="ECO:0000313|EMBL:EPC78253.1"
SQ   SEQUENCE   343 AA;  39910 MW;  9C18E1775E424D89 CRC64;
     MSDLKMGFRW FGEKDDPITL QQIRQIPGTQ QVVGALYDVP VGEVWPKEKI AALKKQVEDA
     GLKLEVIESV NIHDDIKIGL PSRDKYIENY KETIKNLSEY GIKVICYNFM PIFDWLRTNL
     HYQLEDGSNV MAFQHQYLKD DPHDIIESVR NNSEGYVLPG WEPERLAEIE RLFKAYADVD
     AAKLRENMKY FLDAIIPTCE QYDVRMAMHP DDPPRELFDL PRVYKNAEDM RIIEAMHESR
     YNGFTICTGS LGENPKNDVP AIIREFVKKD RAPFIHARNI KFMNKEGDFH ESDHLSKDGS
     LDMYEIMKAL HDLDYDGYIR PDHGRNIWGE NGRPGYGLYD RAL
//
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