ID A0A317VUS2_ASPEC Unreviewed; 270 AA.
AC A0A317VUS2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase {ECO:0000313|EMBL:PWY75620.1};
GN ORFNames=BO83DRAFT_377463 {ECO:0000313|EMBL:PWY75620.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY75620.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY75620.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY75620.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY75620.1}.
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; MSFU01000009; PWY75620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VUS2; -.
DR VEuPathDB; FungiDB:BO83DRAFT_377463; -.
DR OrthoDB; 2785075at2759; -.
DR Proteomes; UP000246171; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF9; HPCH_HPAI ALDOLASE_CITRATE LYASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
FT DOMAIN 34..227
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
SQ SEQUENCE 270 AA; 29063 MW; DADEC35E02E5C2B2 CRC64;
MTYTKTYPTP LTTEISNPRL RLLNKIKAGE YPLMTFMALP SVRMAQIVAL TGVDGIIIDC
EHGHISDDAM HNSVAAISSL GVSPIIRIRG PTHDIVKRAL DTGAHGIMVP QINTVEEAQQ
VVASAKFPPQ GLRGQGSAFP AIGHGLTTPE YMKSANETII TMIQIETRAG VENVDAICAV
PGVDLVFIGP NDLAQSLLGY VPARGDEPEF VAAVEKIVTA ARKHGKWAGR MVNNGTLAKE
ARKTYDTVAI TGDTKAIQNW YMAEFEVARS
//
