ID   A0A1P8WX87_9SPHN        Unreviewed;       403 AA.
AC   A0A1P8WX87;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE            EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
GN   ORFNames=BWQ93_09340 {ECO:0000313|EMBL:APZ98677.1};
OS   Sphingopyxis sp. QXT-31.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1357916 {ECO:0000313|EMBL:APZ98677.1, ECO:0000313|Proteomes:UP000188055};
RN   [1] {ECO:0000313|EMBL:APZ98677.1, ECO:0000313|Proteomes:UP000188055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QXT-31 {ECO:0000313|EMBL:APZ98677.1,
RC   ECO:0000313|Proteomes:UP000188055};
RA   Liang J.S.;
RT   "Microbe-microbe interactions indirectly alter the fate of arsenic in
RT   presence of MnII.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dehydration of D-mannonate. Has no detectable
CC       activity with a panel of 70 other acid sugars (in vitro).
CC       {ECO:0000256|ARBA:ARBA00023758}.
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion. {ECO:0000256|ARBA:ARBA00004892}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GalD subfamily. {ECO:0000256|ARBA:ARBA00010339}.
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DR   EMBL; CP019449; APZ98677.1; -; Genomic_DNA.
DR   RefSeq; WP_077030305.1; NZ_CP019449.1.
DR   AlphaFoldDB; A0A1P8WX87; -.
DR   STRING; 1357916.BWQ93_09340; -.
DR   KEGG; sphq:BWQ93_09340; -.
DR   OrthoDB; 9802699at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000188055; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR034589; D-mannonate_dehydratase-like.
DR   InterPro; IPR034593; DgoD-like.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR034587; MAND.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF6; STARVATION-SENSING PROTEIN RSPA; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00001; mannonate_dehydratase; 1.
DR   SFLD; SFLDG00033; mannonate_dehydratase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188055}.
FT   DOMAIN          129..258
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   403 AA;  44405 MW;  6CCFF00AEE903E02 CRC64;
     MPKIVSARVI VTSPSRNFVT LKIACDDGTT GVGDATLNGR ELAVAAYLSE HVVPCLIGRD
     AHAINDNWHY LYKGAYWRRG PVTMTAIAAV DMALWDIKGK VAGLPVYQLL GGAARDGCMV
     YGHANGETIA DTIEAALEYQ RQGYKAIRLQ CGVPGMASTY GVSKDRYFYE PADAALPSEN
     RWSTEKYLRV VPELFAAARE ALGWDVHLLH DVHHRLTPIE AGRLGKDLEP WRPFWIEDAT
     PAEDQDAFRL IRQHTTAPLA VGEIFNSVWD CKALIENRLI DYIRATVLHA GGITHMRQIA
     SLAELHQVRT GCHGATDLSP VTMAAALHLG ISIPNFGIQE YMRHTADTDA VFPHAYSFAD
     GMLHPGDAPG LGIDIDESLA ETFPYARAYL PVNRLEDGTM WSW
//