ID A0A5N6ZTN1_9EURO Unreviewed; 298 AA.
AC A0A5N6ZTN1;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Dihydrodipicolinate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BDV27DRAFT_149446 {ECO:0000313|EMBL:KAE8359610.1};
OS Aspergillus caelatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=61420 {ECO:0000313|EMBL:KAE8359610.1, ECO:0000313|Proteomes:UP000326268};
RN [1] {ECO:0000313|EMBL:KAE8359610.1, ECO:0000313|Proteomes:UP000326268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 763.97 {ECO:0000313|EMBL:KAE8359610.1,
RC ECO:0000313|Proteomes:UP000326268};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; ML737816; KAE8359610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6ZTN1; -.
DR OrthoDB; 1705410at2759; -.
DR Proteomes; UP000326268; 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:UP000326268}.
FT ACT_SITE 138
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 165
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 50
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 207
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 298 AA; 31826 MW; 175078D1F3DACD57 CRC64;
MSNQELTGVM VALITPFTDD GGKIDESRLK SHIDRLLQAG VHGLVPGGST GEFTVLSLAE
RKQLTELCVK YAAGRVPVVA GTGATSTQEA VELAKHAAEV GAAAVMVVPP YYDPVNYEQL
TEMMSEIHTE SKLPIMYYNI PSASGLTLTP QQLADLSKVG VKYMKDTSGN APAYTELVFA
LSDKITAFNG WDTLTFYGMA AGAPGCVWGA ANVIPELAVQ LWDAIAVKGD LKRGRELWTK
AYPICKFLES HNYAAAVKTG VELTGQPTGG LRKPFALLAD QHKAELASFM QSAGIKTV
//
