MAND1_CAUSK
ID MAND1_CAUSK Reviewed; 403 AA.
AC B0T0B1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=D-mannonate dehydratase Caul1427;
DE Short=ManD;
DE EC=4.2.1.8;
GN OrderedLocusNames=Caul_1427;
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 X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP 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 2.0 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; ABZ70557.1; -; Genomic_DNA.
DR RefSeq; WP_012285484.1; NC_010338.1.
DR PDB; 4FI4; X-ray; 2.00 A; A/B/C=1-403.
DR PDBsum; 4FI4; -.
DR AlphaFoldDB; B0T0B1; -.
DR SMR; B0T0B1; -.
DR STRING; 366602.Caul_1427; -.
DR EnsemblBacteria; ABZ70557; ABZ70557; Caul_1427.
DR KEGG; cak:Caul_1427; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_5; -.
DR OMA; DWDTRAY; -.
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 3D-structure; Carbohydrate metabolism; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..403
FT /note="D-mannonate dehydratase Caul1427"
FT /id="PRO_0000429876"
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:0000269|PubMed:24697546"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
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"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 81..102
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 114..128
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 184..202
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4FI4"
FT TURN 287..291
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:4FI4"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:4FI4"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:4FI4"
SQ SEQUENCE 403 AA; 44661 MW; F537D42E106B83A3 CRC64;
MLKIIDAKVI VTCPGRNFVT LKITTSDGVT GVGDATLNGR ELAVVSYLRD HMIPCLIGRD
AHRIEDVWQF FYRGSYWRGG PVAMTALAAV DMALWDIKAK LAGMPLYQLL GGACREGVMV
YGHANGETIE DTIAEARKYQ ALGYKAIRLQ SGVPGLPSTY GVSGDKMFYE PADGNLPTEN
VWSTSKYLKH APKLFEAARE ALGDDVHLLH DVHHRLTPIE AGRLGKDLEP YRLFWLEDAV
PAENQAGFRL IRQHTTTPLA VGEIFSHVWD CKQLIEEQLI DYLRATVLHA GGITNLRKIA
AFADLHHVRT GCHGATDLSP ITMAAALHFD LSVSNFGLQE YMRHTPETDA VFPHAYSYKD
GMLHPGEAPG LGVDIDEALA GQYPYKRAYL PVNRLEDGTM YNW
