MAND1_CAUVC
ID MAND1_CAUVC Reviewed; 403 AA.
AC Q9A4L8;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=D-mannonate dehydratase CC2812;
DE Short=ManD;
DE EC=4.2.1.8;
GN OrderedLocusNames=CC_2812;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 19089 / CB15;
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 0.65 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; AE005673; AAK24776.1; -; Genomic_DNA.
DR PIR; D87597; D87597.
DR RefSeq; NP_421608.1; NC_002696.2.
DR RefSeq; WP_010920653.1; NC_002696.2.
DR AlphaFoldDB; Q9A4L8; -.
DR SMR; Q9A4L8; -.
DR STRING; 190650.CC_2812; -.
DR EnsemblBacteria; AAK24776; AAK24776; CC_2812.
DR KEGG; ccr:CC_2812; -.
DR PATRIC; fig|190650.5.peg.2814; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_5; -.
DR OMA; EYMRHTE; -.
DR BioCyc; CAULO:CC2812-MON; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000001816; Chromosome.
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;
KW Reference proteome.
FT CHAIN 1..403
FT /note="D-mannonate dehydratase CC2812"
FT /id="PRO_0000429878"
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; 44893 MW; 976518D793811ECA CRC64;
MPKIIAAKTI VTCPGRNFVT LKIMTDEGVY GLGDATLNGR ELAVEAYLTQ HVIPCLIGRD
AHQIEDIWQY LYRGCYWRRG PVTMAAIAAV DTALWDIKGK IAGLPVYQLL GGACRVGVMV
YGHANGETID ETLDNAAVYA QQGYKAIRLQ TGVPGMSGTY GVSKDKFFYE PADSDLPKET
IWSTERYLRS TPALFEAARE RLGDDLHLLH DVHHRLTPIE AARLGKDLEP YRLFWMEDAT
PAENQASFRL IRQHTTTPLA VGEIFNSIWD CKQLIEEQLI DYIRATVVHA GGITHLKKLA
SFADLHHVRT GCHGATDLSP VCMGAALHFD LSIPNFGVQE YMRHTPETDA VFPHAYTFKD
GMLHPGDAPG LGVDIDEDLA AKYPYQRAYL PIARRLDGSM HDW
