ID   LGA1_HYPJE              Reviewed;         315 AA.
AC   A6Y9S5;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=L-threo-3-deoxy-hexylosonate aldolase;
DE            EC=4.1.2.54;
DE   AltName: Full=L-threo-3-deoxy-hexulosonate aldolase;
GN   Name=lga1; Synonyms=kdg1;
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], PROTEIN SEQUENCE OF 44-59; 77-91; 104-119 AND
RP   277-287, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=VTT-D-80133;
RX   PubMed=17609199; DOI=10.1074/jbc.m704401200;
RA   Hilditch S., Berghall S., Kalkkinen N., Penttila M., Richard P.;
RT   "The missing link in the fungal D-galacturonate pathway: identification of
RT   the L-threo-3-deoxy-hexulosonate aldolase.";
RL   J. Biol. Chem. 282:26195-26201(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CBS 383.78;
RX   PubMed=18768163; DOI=10.1016/j.fgb.2008.08.002;
RA   Martens-Uzunova E.S., Schaap P.J.;
RT   "An evolutionary conserved d-galacturonic acid metabolic pathway operates
RT   across filamentous fungi capable of pectin degradation.";
RL   Fungal Genet. Biol. 45:1449-1457(2008).
CC   -!- FUNCTION: Mediates the conversion of 2-dehydro-3-deoxy-L-galactonate to
CC       pyruvate and L-glyceraldehyde in D-galacturonate catabolic process.
CC       {ECO:0000269|PubMed:17609199, ECO:0000269|PubMed:18768163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-L-galactonate = L-glyceraldehyde + pyruvate;
CC         Xref=Rhea:RHEA:38107, ChEBI:CHEBI:15361, ChEBI:CHEBI:27975,
CC         ChEBI:CHEBI:75545; EC=4.1.2.54;
CC         Evidence={ECO:0000269|PubMed:17609199};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.5 mM for 2-dehydro-3-deoxy-L-galactonate
CC         {ECO:0000269|PubMed:17609199};
CC         KM=3.8 mM for D-glycero-3-deoxy-pentulosonate
CC         {ECO:0000269|PubMed:17609199};
CC         KM=0.5 mM for pyruvate {ECO:0000269|PubMed:17609199};
CC         KM=1.2 mM for L-glyceraldehyde {ECO:0000269|PubMed:17609199};
CC         KM=6.5 mM for glycolaldehyde {ECO:0000269|PubMed:17609199};
CC         Vmax=20.3 umol/min/mg enzyme with 2-dehydro-3-deoxy-L-galactonate as
CC         substrate {ECO:0000269|PubMed:17609199};
CC         Vmax=12.5 umol/min/mg enzyme with D-glycero-3-deoxy-pentulosonate as
CC         substrate {ECO:0000269|PubMed:17609199};
CC         Vmax=6.5 umol/min/mg enzyme with pyruvate and L-glyceraldehyde as
CC         substrates {ECO:0000269|PubMed:17609199};
CC         Vmax=0.9 umol/min/mg enzyme with glycolaldehyde as substrate
CC         {ECO:0000269|PubMed:17609199};
CC   -!- PATHWAY: Carbohydrate acid metabolism. {ECO:0000269|PubMed:17609199}.
CC   -!- DISRUPTION PHENOTYPE: Cells are unable to grow on D-galacturonate.
CC       {ECO:0000269|PubMed:17609199}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
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DR   EMBL; EF203091; ABP04235.1; -; mRNA.
DR   EMBL; EF563987; ABQ53584.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6Y9S5; -.
DR   SMR; A6Y9S5; -.
DR   KEGG; ag:ABP04235; -.
DR   OMA; YYGYGGF; -.
DR   BioCyc; MetaCyc:MON-15605; -.
DR   BRENDA; 4.1.2.54; 6451.
DR   SABIO-RK; A6Y9S5; -.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IDA:UniProtKB.
DR   GO; GO:0019698; P:D-galacturonate catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Lyase.
FT   CHAIN           1..315
FT                   /note="L-threo-3-deoxy-hexylosonate aldolase"
FT                   /id="PRO_0000425569"
FT   ACT_SITE        174
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            145
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        51
FT                   /note="N -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   315 AA;  33407 MW;  E6979A0B24A88AA7 CRC64;
     MAPPSLPCGI YAPTMTFFHP ESEDIDIPTI KHHAQRLAKA GLAGLVVMGS NGEAVHCTRD
     EKIAVLSATR EALDAAGFQS VPVLFGATEG SVRGTIELCK LAAAAGAAAA LVLPPSYYRA
     QTDEASIEAY FVAVADASPI PLVLYNYPGA VSGIDMDSDL LIRLAQHKNI VGTKFTCGNT
     GKLTRVALAT DAKTPFRDGS GYMAFGGMCD FTLQTLVSGG SGIIAGGANV MPKLCVKVWD
     SYSQGNRDEA EKLQKVLSRG DWPLTKAAIA GTKSAIQTYY GYGGYPRRPL KRLEQARVSA
     IEEGIREAME IEKTL