ID A0A9J9HBD0_RHIWR Unreviewed; 402 AA.
AC A0A9J9HBD0;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=D-mannonate dehydratase {ECO:0000256|ARBA:ARBA00074797};
DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
GN OrderedLocusNames=Swit_1889 {ECO:0000313|EMBL:ABQ68249.1};
OS Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS 105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=392499 {ECO:0000313|EMBL:ABQ68249.1, ECO:0000313|Proteomes:UP000001989};
RN [1] {ECO:0000313|EMBL:ABQ68249.1, ECO:0000313|Proteomes:UP000001989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1
RC {ECO:0000313|Proteomes:UP000001989};
RX PubMed=20833805; DOI=10.1128/JB.01030-10;
RA Miller T.R., Delcher A.L., Salzberg S.L., Saunders E., Detter J.C.,
RA Halden R.U.;
RT "Genome sequence of the dioxin-mineralizing bacterium Sphingomonas
RT wittichii RW1.";
RL J. Bacteriol. 192:6101-6102(2010).
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; CP000699; ABQ68249.1; -; Genomic_DNA.
DR KEGG; swi:Swit_1889; -.
DR OrthoDB; 9802699at2; -.
DR Proteomes; UP000001989; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA.
DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:InterPro.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd03322; RspA; 1.
DR FunFam; 3.20.20.120:FF:000004; D-galactonate dehydratase family protein; 1.
DR FunFam; 3.30.390.10:FF:000002; D-galactonate dehydratase family protein; 1.
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; IPR053379; D-mannonate_dehydratase_GalD.
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 NCBIfam; NF043051; ManoateDhtManD; 1.
DR NCBIfam; NF011654; PRK15072.1; 1.
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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000001989}.
FT DOMAIN 128..257
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 402 AA; 45173 MW; 47F86B51AECA01AA CRC64;
MRIDAAKVIV TCPGRNFVTV KIMTDQGVHG VGDATLNGRE LSVASYLQDH LLPCLIGRDP
RRIEDIWQYF YRGAYWRRGP VTMSAIAAID MALWDIKAKM ANMPLYDLLG GKSREGVMVY
GHANGADIEQ TIDEVGRYIS LGYRAIRAQS GIPGLAAAYG VGRGKDYYEP ADAALPTETV
WDTAKYLNFV PKLFDKLRDR YGFEHHLLHD VHHRLRPIEA GRLGKMLEPY GLFWLEDATP
AENQEAFRLI RQHTTIPLAV GEVFNTVWDC KDLIQNQLID YIRTPVVRAG GITHLRRIAD
LAALYQVQTG FHGATDLSPV TMGTALHFDS WVPNFGIQEY MRHTPETDAV FPHAYHFADG
YLHPGDAIGH GVDIDEAEAA KYPYKPAYLP VARLEDGTMF NW
//
