ID W4KJQ4_HETIT Unreviewed; 347 AA.
AC W4KJQ4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Dihydrodipicolinate synthetase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HETIRDRAFT_448998 {ECO:0000313|EMBL:ETW86093.1};
OS Heterobasidion irregulare (strain TC 32-1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Bondarzewiaceae; Heterobasidion;
OC Heterobasidion annosum species complex.
OX NCBI_TaxID=747525 {ECO:0000313|EMBL:ETW86093.1, ECO:0000313|Proteomes:UP000030671};
RN [1] {ECO:0000313|EMBL:ETW86093.1, ECO:0000313|Proteomes:UP000030671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC 32-1 {ECO:0000313|EMBL:ETW86093.1,
RC ECO:0000313|Proteomes:UP000030671};
RX PubMed=22463738; DOI=10.1111/j.1469-8137.2012.04128.x;
RA Olson A., Aerts A., Asiegbu F., Belbahri L., Bouzid O., Broberg A.,
RA Canback B., Coutinho P.M., Cullen D., Dalman K., Deflorio G.,
RA van Diepen L.T., Dunand C., Duplessis S., Durling M., Gonthier P.,
RA Grimwood J., Fossdal C.G., Hansson D., Henrissat B., Hietala A.,
RA Himmelstrand K., Hoffmeister D., Hogberg N., James T.Y., Karlsson M.,
RA Kohler A., Kues U., Lee Y.H., Lin Y.C., Lind M., Lindquist E., Lombard V.,
RA Lucas S., Lunden K., Morin E., Murat C., Park J., Raffaello T., Rouze P.,
RA Salamov A., Schmutz J., Solheim H., Stahlberg J., Velez H., de Vries R.P.,
RA Wiebenga A., Woodward S., Yakovlev I., Garbelotto M., Martin F.,
RA Grigoriev I.V., Stenlid J.;
RT "Insight into trade-off between wood decay and parasitism from the genome
RT of a fungal forest pathogen.";
RL New Phytol. 194:1001-1013(2012).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI925455; ETW86093.1; -; Genomic_DNA.
DR RefSeq; XP_009542869.1; XM_009544574.1.
DR AlphaFoldDB; W4KJQ4; -.
DR STRING; 747525.W4KJQ4; -.
DR GeneID; 20675903; -.
DR KEGG; hir:HETIRDRAFT_448998; -.
DR eggNOG; ENOG502QWNS; Eukaryota.
DR HOGENOM; CLU_049343_0_2_1; -.
DR InParanoid; W4KJQ4; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000030671; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; 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 PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000030671}.
FT ACT_SITE 157
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 187
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 243
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 347 AA; 36425 MW; 9B7D62C67154038F CRC64;
MALNGSNGVH SSVTRPLQPG IFAPIPTFFF PDTEDLDIAS FESHIVRLAQ ANVGPLLAGS
MGEALHLSHE ERKTLIKAAR GALDAAGFTH VPIIAGTGAG STRETIQLNK EAADAGADYA
IVITSGYFAG VLASNRKALK DFYAEVSEKS PISIIIYNYP GASGGIDLDS DLITEIATDC
PNTCGVKLTC GSVGKLTRIC ATVSDPSFAS AHPRRNAAAP FLVLGGFTDF IVASTFANGH
GAITGLANVA PYAVAKLFEV SVLAFKDPSF LAEAQRLQGV IACADFTIAK ASISGTKYLL
EKLYGYGGLP RRPLPPIEPK AAEALWLHPH TQDLVKLERS LSGKVVS
//