MAND_ESCAT
ID MAND_ESCAT Reviewed; 404 AA.
AC B1ELW6;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
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; ORFNames=ESCAB7627_2604;
OS Escherichia albertii (strain TW07627).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=502347;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW07627;
RA Sutton G., Whittam T.S., Sebastian Y.;
RT "Annotation of Escherichia albertii TW07627.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=TW07627;
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; ABKX01000005; EDS91725.1; -; Genomic_DNA.
DR RefSeq; WP_002462119.1; NZ_CH991859.1.
DR AlphaFoldDB; B1ELW6; -.
DR SMR; B1ELW6; -.
DR STRING; 502347.ESCAB7627_2604; -.
DR PRIDE; B1ELW6; -.
DR EnsemblBacteria; EDS91725; EDS91725; ESCAB7627_2604.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_6; -.
DR Proteomes; UP000003042; Unassembled WGS sequence.
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 Lyase; Magnesium; Metal-binding.
FT CHAIN 1..404
FT /note="D-galactonate dehydratase family member RspA"
FT /id="PRO_0000429887"
FT ACT_SITE 159
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
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 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 316
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"
SQ SEQUENCE 404 AA; 46040 MW; A609A0E767AA49D8 CRC64;
MKIVRAEVFV TCPGRNFVTL KITTEDGITG LGDATLNGRE LSVASYLQDH LCPQLIGRDA
HRIEDIWQFF YKGAYWRRGP VTMSAISAVD MALWDIKAKV ANMPLYQLLG GASREGVMVY
CHTTGHSIEE ALDDYARHQE LGFKAIRVQC GIPGMKTTYG MSKGKGLAYE PATKGQWPEE
QLWSTEKYLD FMPKLFDAVR NKFGFDEHLL HDMHHRLTPI EAARFGKSIE DYRMFWMEDP
TPAENQECFR LIRQHTVTPI AVGEVFNSIW DCKQLIEEQL IDYIRTTLTH AGGITGMRRI
ADFASLYQVR TGSHGPSDLS PVCMAAALHF DLWVPNFGVQ EYMGYSEQML EVFPHNWTFD
NGYMHPGDKP GLGIEFDEKL AAKYPYEPAY LPVARLEDGT LWNW
