ID A0A0F0I4C1_ASPPU Unreviewed; 301 AA.
AC A0A0F0I4C1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Dihydrodipicolinate synthase family protein {ECO:0000313|EMBL:KJK61462.1};
GN ORFNames=P875_00042360 {ECO:0000313|EMBL:KJK61462.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61462.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK61462.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJK61462.1}.
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DR EMBL; JZEE01000675; KJK61462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0I4C1; -.
DR STRING; 1403190.A0A0F0I4C1; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00665; DHDPS_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT ACT_SITE 141
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 168
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 53
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 210
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 301 AA; 32714 MW; 03F3093AEFE53FD5 CRC64;
MTRTTPVQLT GILTALITPF TDDGSSIDAA RLKAHIDRQF DAGIHGLVPG GSTGEFTTLT
NEERKQLVEL TVKYTAGRGP VIAGVGSTKS AEAIELAVHA AQAGADAVMV VPPFYDPVNY
EQLQELLNEI HEASKLPILY YNIPSASGLT LSPEQIAGLS QVGVKWFKDT SGNAPDFTEL
VFKYGNQVKA MNGWDTLTFY GIAAGNEAVI WGAANFIPEL AVELWNTLAV KNDLRRGREL
WASIWPITKF LESHNYAAAV KSGVELRGLK TGGLRKPFAL LKEEHQLELQ QLLLTAQVKL
N
//
