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Database: UniProt
Entry: L7ZSH1_9BACI
LinkDB: L7ZSH1_9BACI
Original site: L7ZSH1_9BACI 
ID   L7ZSH1_9BACI            Unreviewed;       371 AA.
AC   L7ZSH1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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:AGE22448.1};
GN   ORFNames=GHH_c19300 {ECO:0000313|EMBL:AGE22448.1};
OS   Geobacillus sp. GHH01.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1233873 {ECO:0000313|EMBL:AGE22448.1, ECO:0000313|Proteomes:UP000011251};
RN   [1] {ECO:0000313|EMBL:AGE22448.1, ECO:0000313|Proteomes:UP000011251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHH01 {ECO:0000313|EMBL:AGE22448.1};
RX   PubMed=23618712;
RA   Wiegand S., Rabausch U., Chow J., Daniel R., Streit W.R., Liesegang H.;
RT   "Complete Genome Sequence of Geobacillus sp. Strain GHH01, a Thermophilic
RT   Lipase-Secreting Bacterium.";
RL   Genome Announc. 1:E0009213-E0009213(2013).
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}.
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DR   EMBL; CP004008; AGE22448.1; -; Genomic_DNA.
DR   RefSeq; WP_015374971.1; NC_020210.1.
DR   AlphaFoldDB; L7ZSH1; -.
DR   KEGG; ggh:GHH_c19300; -.
DR   PATRIC; fig|1233873.3.peg.2064; -.
DR   HOGENOM; CLU_058621_1_0_9; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000011251; Chromosome.
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   371 AA;  42531 MW;  D582785FACDAE944 CRC64;
     MKMTFRWFGK EHDTVSLDHI RQIPGVEGIV GALYHIPVGE VWPLDDILEL KRQVNEKGFH
     LEVIESVNVH EDIKLGLPSR DRYIENYKQT IRNLAKAGVK VICYNFMPIF DWTRSDLAKR
     RPDGSTVLAY EKQKIEQIDP EEMIRRIESG ANGFLLPGWE PERLKTIKPL FSLYKGVTEE
     DLFDHLRYFL EQIVPVAEEC GVRMALHPDD PPWSVFGLPR IATNKENLDR IVHMVNSPAN
     GLTLCSGSLG ANPANDVPDI FRHFLRMGRV PFAHVRNVEI HANGDFEETS HRSCDGSLNI
     CEIMKALHEA NFQGYIRPDH GRMIWGEQAR PGYGLYDRAL GIMYLLGIWD SLENKKKKQE
     GEKTCSRSIQ V
//
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