ID   MAND_STRS3              Reviewed;         442 AA.
AC   D9UNB2;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=D-galactonate dehydratase family member SSLG_02014;
DE            EC=4.2.1.-;
DE   AltName: Full=D-mannonate dehydratase;
DE            EC=4.2.1.8;
GN   ORFNames=SSLG_02014;
OS   Streptomyces sp. (strain SPB78).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=591157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPB78;
RG   The Broad Institute Genome Sequencing Platform, Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain SPB78.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=SPB78;
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 0.004 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; GG657742; EFK99955.1; -; Genomic_DNA.
DR   RefSeq; WP_009065588.1; NZ_GG657742.1.
DR   AlphaFoldDB; D9UNB2; -.
DR   SMR; D9UNB2; -.
DR   STRING; 591157.SSLG_02014; -.
DR   EnsemblBacteria; EFK99955; EFK99955; SSLG_02014.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_6_1_11; -.
DR   Proteomes; UP000005781; 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   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   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..442
FT                   /note="D-galactonate dehydratase family member SSLG_02014"
FT                   /id="PRO_0000429891"
FT   ACT_SITE        197
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        248
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            350
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   442 AA;  47830 MW;  2B0DD09F00017E8F CRC64;
     MASSAHSDSA SADASAEIPA EILAPAPWST PADDSEHLRI TAVRTFLTAP QGCPYVIVRV
     ETNQPGLYGL GCASDPQRTL AIRSVVDDYY APMLLGRDPS DIEDLHRLLF NSGYWRGGSI
     GQNALAGVDV ALWDIKGKVA GLPLHQLLGG RAREAADAYT HVDGDNAGEI AEKVLAAHER
     GYRHVRVQVS VPGTDTYGTA PRDAAEARRR ELRAGSWDSL AYLRHVPPVL REIRERVGTG
     VELLHDAHER LTPSQARELV HEVEDARLFF LEDALAPEDA AHFDQLRAAG SVPLAVGELY
     HDVMMYLPLL QRQVIDFARI RIPTLGGLTP TRKLVAAVEL FGARTAPHGP GDVSPVGMAA
     NLGLDLSSPA FGVQEAATFR EATREVFPGT PVPERGRFHG TGLPGLGVDF DEAAARKYPV
     PEPLRHDRWA LLRNGDGSVQ RP