MAND_ECOL6
ID MAND_ECOL6 Reviewed; 415 AA.
AC Q8FHC7;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=c1971;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL 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 0.02 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; AE014075; AAN80431.1; -; Genomic_DNA.
DR PDB; 4IL2; X-ray; 1.95 A; A/B/C/D=1-415.
DR PDBsum; 4IL2; -.
DR AlphaFoldDB; Q8FHC7; -.
DR SMR; Q8FHC7; -.
DR STRING; 199310.c1971; -.
DR PRIDE; Q8FHC7; -.
DR EnsemblBacteria; AAN80431; AAN80431; c1971.
DR KEGG; ecc:c1971; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_6; -.
DR OMA; DWDTRAY; -.
DR BioCyc; ECOL199310:C1971-MON; -.
DR Proteomes; UP000001410; 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.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..415
FT /note="D-galactonate dehydratase family member RspA"
FT /id="PRO_0000429885"
FT ACT_SITE 170
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 327
FT /note="Important for activity and substrate specificity;
FT Pro is observed in family members with low D-mannonate
FT dehydratase activity"
FT /evidence="ECO:0000250"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 91..111
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4IL2"
FT TURN 299..303
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:4IL2"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:4IL2"
FT HELIX 389..393
FT /evidence="ECO:0007829|PDB:4IL2"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:4IL2"
SQ SEQUENCE 415 AA; 47350 MW; D2170A630D547E9B CRC64;
MHHDKRCKES NMKIVKAEVF VTCPGRNFVT LKITTEDGIT GLGDATLNGR ELSVASYLQD
HLCPQLIGRD AHRIEDIWQF FYKGAYWRRG PVTMSAISAV DMALWDIKAK AANMPLYQLL
GGASREGVMV YCHTTGHSID EALDDYARHQ ELGFKAIRVQ CGIPGMKTTY GMSKGKGLAY
EPATKGQWPE EQLWSTEKYL DFMPKLFDAV RNKFGFDEHL LHDMHHRLTP IEAARFGKSI
EDYRMFWMED PTPAENQECF RLIRQHTVTP IAVGEVFNSI WDCKQLIEEQ LIDYIRTTLT
HAGGITGMRR IADFASLYQV RTGSHGPSDL SPVCMAAALH FDLWVPNFGV QEYMGYSEQM
LEVFPHNWTF DNGYMHPGEK PGLGIEFDEK LAAKYPYEPA YLPVARLEDG TLWNW
