MAND2_CAUSK
ID MAND2_CAUSK Reviewed; 403 AA.
AC B0T4L2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=D-mannonate dehydratase Caul1835;
DE Short=ManD;
DE EC=4.2.1.8;
GN OrderedLocusNames=Caul_1835;
OS Caulobacter sp. (strain K31).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX NCBI_TaxID=366602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K31;
RX PubMed=24697546; DOI=10.1021/bi500264p;
RA Wichelecki D.J., Balthazor B.M., Chau A.C., Vetting M.W., Fedorov A.A.,
RA Fedorov E.V., Lukk T., Patskovsky Y.V., Stead M.B., Hillerich B.S.,
RA Seidel R.D., Almo S.C., Gerlt J.A.;
RT "Discovery of function in the enolase superfamily: D-mannonate and D-
RT gluconate dehydratases in the D-mannonate dehydratase subgroup.";
RL Biochemistry 53:2722-2731(2014).
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:0000269|PubMed:24697546}.
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:0000269|PubMed:24697546};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24697546};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24697546};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.3 sec(-1) with D-mannonate.
CC {ECO:0000269|PubMed:24697546};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GalD subfamily. {ECO:0000305}.
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DR EMBL; CP000927; ABZ70964.1; -; Genomic_DNA.
DR RefSeq; WP_012285882.1; NC_010338.1.
DR AlphaFoldDB; B0T4L2; -.
DR SMR; B0T4L2; -.
DR STRING; 366602.Caul_1835; -.
DR EnsemblBacteria; ABZ70964; ABZ70964; Caul_1835.
DR KEGG; cak:Caul_1835; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_5; -.
DR OMA; EYMRHTE; -.
DR OrthoDB; 1825548at2; -.
DR UniPathway; UPA00246; -.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008927; F:mannonate dehydratase activity; IDA:CACAO.
DR GO; GO:0016052; P:carbohydrate catabolic process; IDA:UniProtKB.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR034589; D-mannonate_dehydratase-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; IPR034593; Mandelate_racemase_DgoD-like.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080; PTHR48080; 1.
DR PANTHER; PTHR48080:SF6; PTHR48080:SF6; 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; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00908; MR_MLE_1; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..403
FT /note="D-mannonate dehydratase Caul1835"
FT /id="PRO_0000429877"
FT ACT_SITE 160
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 213
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 315
FT /note="Important for activity and substrate specificity;
FT Ala is observed in family members with high D-mannonate
FT dehydratase activity that have no activity with D-
FT gluconate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 403 AA; 44711 MW; 241FD895FF3D344D CRC64;
MPKITAARVV VTCPGRNFVT LKIETSDGVY GVGDATLNGR ELPVVSYLTD HVIPCLIGRD
AHRIEDIWQY LYKGAYWRRG PVTMAAIAAV DMALWDIKAK IAGLPLYQLL GGACREGIMV
YGHANGATIE ETLENAAVYA AQGYKAIRLQ SGVPGLKGVY GVSKDKFFYE PADGDLPTES
LWSTEKYLRS APGLFEAARD KLGWDLHLLH DVHHRLTPIE AGRLGKDLEP YRPFWMEDAV
PAENQASFRL IRQHTTTPLA VGEVFNSIWD CKQLIEEQLI DYIRATVVHA GGITHLRKIA
SFADLHHVRT GCHGATDLSP IAMAAALHFD LSIPNFGIQE YMRHTEATDT VFPHAYTFND
GMLHPGDAVG LGVDINETEA AKYPYKRAYL PIARREDGSM HDW
