ID   LGD1_HYPJE              Reviewed;         450 AA.
AC   Q0QWS4;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=L-galactonate dehydratase;
DE            EC=4.2.1.146;
GN   Name=lgd1;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 56765 / Rut C-30;
RX   PubMed=16879654; DOI=10.1111/j.1365-2958.2006.05294.x;
RA   Kuorelahti S., Jouhten P., Maaheimo H., Penttila M., Richard P.;
RT   "L-galactonate dehydratase is part of the fungal path for D-galacturonic
RT   acid catabolism.";
RL   Mol. Microbiol. 61:1060-1068(2006).
CC   -!- FUNCTION: Mediates the conversion of L-galactonate to 2-dehydro-3-
CC       deoxy-L-galactonate, the second step in D-galacturonate catabolic
CC       process. {ECO:0000269|PubMed:16879654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-galactonate = 2-dehydro-3-deoxy-L-galactonate + H2O;
CC         Xref=Rhea:RHEA:38103, ChEBI:CHEBI:15377, ChEBI:CHEBI:53071,
CC         ChEBI:CHEBI:75545; EC=4.2.1.146;
CC         Evidence={ECO:0000269|PubMed:16879654};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Divalent metal ions. Magnesium seems to be the preferred ion.
CC       {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate acid metabolism. {ECO:0000269|PubMed:16879654}.
CC   -!- DISRUPTION PHENOTYPE: Cells are unable to grow on D-galacturonate.
CC       {ECO:0000269|PubMed:16879654}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. {ECO:0000305}.
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DR   EMBL; DQ181420; ABA60340.1; -; mRNA.
DR   AlphaFoldDB; Q0QWS4; -.
DR   SMR; Q0QWS4; -.
DR   VEuPathDB; FungiDB:TrQ_009564; -.
DR   OMA; SGAIDVC; -.
DR   BioCyc; MetaCyc:MON-15604; -.
DR   BRENDA; 4.2.1.146; 6451.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0050023; F:L-fuconate dehydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0019698; P:D-galacturonate catabolic process; IDA:UniProtKB.
DR   CDD; cd03324; rTSbeta_L-fuconate_dehydratase; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR034610; L-fuconate_dehydratase.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SFLD; SFLDF00111; L-fuconate_dehydratase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..450
FT                   /note="L-galactonate dehydratase"
FT                   /id="PRO_0000425568"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  50124 MW;  786A8E7639A3407C CRC64;
     MSEVTITGFR SRDVRFPTSL DKTGSDAMNA AGDYSAAYCI LETDSAHSGH GMTFTIGRGN
     DIVCAAINHV ADRLKGKKLS SLVADWGKTW RYLVNDSQLR WIGPEKGVIH LALGAVVNAV
     WDLWAKTLNK PVWRIVADMT PEEYVRCIDF RYITDAITPE EAVAMLREQE AGKAKRIEEA
     LQNRAVPAYT TSAGWLGYGE DKMKQLLRET LAAGYRHFKV KVGGSVEEDR RRLGIAREIL
     GFDKGNVLMV DANQVWSVPE AIDYMKQLSE YKPWFIEEPT SPDDIMGHKA IRDALKPYGI
     GVATGEMCQN RVMFKQLIMT GAIDICQIDA CRLGGVNEVL AVLLMAKKYG VPIVPHSGGV
     GLPEYTQHLS TIDYVVVSGK LSVLEFVDHL HEHFLHPSVI KDGYYQTPTE AGYSVEMKPE
     SMDKYEYPGK KGVSWWTTDE ALPILNGEKI