MAND_CELJU
ID MAND_CELJU Reviewed; 402 AA.
AC B3PDB1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=D-galactonate dehydratase family member RspA;
DE EC=4.2.1.-;
DE AltName: Full=D-mannonate dehydratase;
DE EC=4.2.1.8;
DE AltName: Full=Starvation sensing protein RspA homolog;
GN Name=rspA; OrderedLocusNames=CJA_3069;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP TARTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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: Has low D-mannonate dehydratase activity (in vitro),
CC suggesting that this is not a physiological substrate and that it has
CC no significant role in D-mannonate degradation in vivo. Has no
CC detectable 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 0.03 sec(-1) with D-mannonate.
CC {ECO:0000269|PubMed:24697546};
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GalD subfamily. {ECO:0000305}.
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DR EMBL; CP000934; ACE86256.1; -; Genomic_DNA.
DR RefSeq; WP_012488647.1; NC_010995.1.
DR PDB; 3V3W; X-ray; 1.40 A; A=1-402.
DR PDB; 3V4B; X-ray; 1.40 A; A=1-402.
DR PDBsum; 3V3W; -.
DR PDBsum; 3V4B; -.
DR AlphaFoldDB; B3PDB1; -.
DR SMR; B3PDB1; -.
DR STRING; 498211.CJA_3069; -.
DR EnsemblBacteria; ACE86256; ACE86256; CJA_3069.
DR KEGG; cja:CJA_3069; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_6; -.
DR OMA; EYMRHTE; -.
DR OrthoDB; 1825548at2; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008927; F:mannonate dehydratase activity; IDA:UniProtKB.
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; 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; 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; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..402
FT /note="D-galactonate dehydratase family member RspA"
FT /id="PRO_0000429884"
FT ACT_SITE 159
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 80..100
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 183..201
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:3V3W"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:3V3W"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:3V3W"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:3V3W"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:3V3W"
SQ SEQUENCE 402 AA; 45404 MW; C6E84C39FE5EFBB1 CRC64;
MKIVDAKVIV TCPGRNFVTL KIVTDQGIYG IGDATLNGRE KSVVSYLEDY LIPVLIGRDP
QQIEDIWQFF YRGAYWRRGP VGMTALAAID VALWDIKAKL ANMPLYQLLG GKSRERILSY
THANGKDLDS TLEAVRKAKD KGYKAIRVQC GIPGIAKTYG VSTNTKSYEP ADADLPSVEV
WSTEKYLNYI PDVFAAVRKE FGPDIHLLHD VHHRLTPIEA ARLGKALEPY HLFWMEDAVP
AENQESFKLI RQHTTTPLAV GEVFNSIHDC RELIQNQWID YIRTTIVHAG GISQMRRIAD
FASLFHVRTG FHGATDLSPV CMGAALHFDY WVPNFGIQEH MAHSEQMNAV FPHAYTFNDG
YFTPGEKPGH GVDIDEKLAA QYPYKRACLP VNRLEDGTLW HW
