ID A1C790_ASPCL Unreviewed; 365 AA.
AC A1C790;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:EAW14261.1};
GN ORFNames=ACLA_072950 {ECO:0000313|EMBL:EAW14261.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14261.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW14261.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027045; EAW14261.1; -; Genomic_DNA.
DR RefSeq; XP_001275687.1; XM_001275686.1.
DR AlphaFoldDB; A1C790; -.
DR STRING; 344612.A1C790; -.
DR EnsemblFungi; EAW14261; EAW14261; ACLA_072950.
DR GeneID; 4708131; -.
DR KEGG; act:ACLA_072950; -.
DR VEuPathDB; FungiDB:ACLA_072950; -.
DR eggNOG; ENOG502QWNS; Eukaryota.
DR HOGENOM; CLU_049343_0_2_1; -.
DR OMA; IAPKACI; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
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:SF52; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 38916 MW; F06367AD4025E866 CRC64;
MSTHLDIPAR MAELGQTDTT TTTTTSTPST IYSHCHRNPT YSSTTLAPSE EHPRRILKPG
LYVPTLASFS PETEEVDEST TAQHAVRMAK AGVMGLITHG TYGEAAHLSH TERCRITRTT
RHAVAAAGYP QMPIIVGCGA PSTSETIELC QDARDSGGDY ALLLFPSAYM SHYTKASLRR
FFEDVAGASP LPVLIYNYPA VTGVDLDAET IAALAQHPNI VGCKLTCNNM GKLNQIVATV
KPATFSDRGS EFMCFGGSAD AALQAMIGGG SGVIAGLGNV MPKACVKLVE LYHLGRIDEA
RQLQGTVAKA DQVAIEGGVS AVKSALRVFY GYGGYARRPL RSDEKEKEKS ATDGLKEGID
LEKSL
//
