ID E5R1F5_ARTGP Unreviewed; 313 AA.
AC E5R1F5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Dihydrodipicolinate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGYG_00745 {ECO:0000313|EMBL:EFQ97706.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(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; DS989822; EFQ97706.1; -; Genomic_DNA.
DR RefSeq; XP_003176658.1; XM_003176610.1.
DR AlphaFoldDB; E5R1F5; -.
DR STRING; 535722.E5R1F5; -.
DR GeneID; 10031978; -.
DR VEuPathDB; FungiDB:MGYG_00745; -.
DR eggNOG; ENOG502SG3E; Eukaryota.
DR HOGENOM; CLU_049343_0_2_1; -.
DR InParanoid; E5R1F5; -.
DR OMA; VMGLSGY; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000002669; 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; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR PANTHER; PTHR12128:SF47; DIHYDRODIPICOLINATE SYNTHETASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_2G01230); 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:UP000002669}.
FT ACT_SITE 141
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 171
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 214
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 313 AA; 32978 MW; 55C8C552FFD9B18D CRC64;
MLPRVPSAGV WCPAVTFFDP ATDELDLSAQ KEYYAYLARS GLTGLVILGT NAEAFLLTRE
ERAQLISTAR EAVGPDYPLM AGVGGHSTRQ VLQHIQDAVT AGANYVLVLP PAYFGKATTP
AVIRAFFGEV AASSPLPVVI YNFPGVCNGV DLDSEMITTI AQGNPNVVGV KLTCASVGKI
TRLAAVLAAD EFSIFGGQAD FLIGGLSVGS AGCISAFANV FPKTISKVYE LYKAGRVKEA
LSLHQKAALA ESPCKSGIAT TKYAAAIFCA KAAGIENAEE RMRPRRPYEA PTEAAKENVK
KAMAEVALIE QGL
//
