ID   LGA1_ASPNG              Reviewed;         335 AA.
AC   A8DRH7;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 48.
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=gaaC; Synonyms=lga1; ORFNames=An02g07720;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
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: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   -!- PATHWAY: Carbohydrate acid metabolism.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
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DR   EMBL; EF563988; ABQ53586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8DRH7; -.
DR   SMR; A8DRH7; -.
DR   STRING; 5061.CADANGAP00002225; -.
DR   VEuPathDB; FungiDB:An02g07720; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1158310; -.
DR   VEuPathDB; FungiDB:ATCC64974_56460; -.
DR   VEuPathDB; FungiDB:M747DRAFT_280865; -.
DR   eggNOG; ENOG502QWNS; Eukaryota.
DR   BRENDA; 4.1.2.54; 518.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; 2.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Lyase.
FT   CHAIN           1..335
FT                   /note="L-threo-3-deoxy-hexylosonate aldolase"
FT                   /id="PRO_0000425570"
FT   ACT_SITE        175
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            146
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  35845 MW;  7D02DDC2DBC21B2D CRC64;
     MPFTPLRPGV YAPTMTFFDP STEDLDVPTI RKHAVRLAKA GLVGLVCMGS NGEAVHLTRA
     ERKTVINETR SALVEAGFSN VPVIAGASEQ SIRGTIELCK ESYEAGAEYA LIVPPSYYRY
     ATGNDQTLYE FFTSVADGSP IPLILYNYPG AVAGIDMDSD LIIRISQHPN IVGTKFTCAN
     TGKLTRVASA LHAITPPSPL APAQRKFPST KTEANHPYVA FGGIADFSLQ TLASGGSAIL
     AGGANVIPKL CVQIFNLWSA GRFTEAMEAQ ELLSRADWVL TKAAIPGTKS AIQSYYGYGG
     FPRRPLARLS AEQAEAVAEK IKDAMEVEKS LPDIA