ID A0A2H3IQJ7_9EURO Unreviewed; 560 AA.
AC A0A2H3IQJ7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Aconitase/3-isopropylmalate dehydratase, swivel {ECO:0000313|EMBL:PCG95880.1};
GN ORFNames=PENO1_071160 {ECO:0000313|EMBL:PCG95880.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG95880.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG95880.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG95880.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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:PCG95880.1}.
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DR EMBL; NPFK01000229; PCG95880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IQJ7; -.
DR STRING; 290292.A0A2H3IQJ7; -.
DR OrthoDB; 238at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR037237; IlvD/EDD_N.
DR PANTHER; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00920; ILVD_EDD; 2.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 60095 MW; 7153F9DC8366BD55 CRC64;
MSLPSNNKDQ NDNNNTTTPQ DDYNLTTPLT TTTGLRQGLT SYGDAHFSLF LRKVFIKALG
YTDSALSRPL IGIINTYSSY NPCHANVPQL IEATKRGVQL AGGLAIDFPT ITLHESFAYP
TSMFLRNLMS MDTEEMIRAQ PMDGNNWAAY RAGTIDVEEI SAINEELAPT SGTCGVMGTA
STMACLTAAL GMMPLKGASA PAVSSARLRI AEETGSNAVA VAIANRTPQD ILSEESFLNA
ITVLQAIGGS TNAVVHLLAI ANRHPAIKGK ITLQTFDDIG RKTPLLIDLK PSGANYMTDF
HNAGGMLALL HTLRPLLHLN AMTMSGKTLG EVLDESPFKS FAYSREVIRS LDNPLYPSSS
LVVLRGNIAP NGAVMKASAS KDRSLLKHSG PAVVFEDTAD MARRIDDPDL PVTKDSVLVL
KGIGPVGNPG MPEAGLIPLP RKLGAQGVTD MLRLSDGRMS GTAGGTIILH ISPESALPES
PFGVVRTGDV ITCDVEQRRL HLEVSDEEIE RRVAERRKDI ERSVGEKKSQ RGYRGLYIRS
VNQAEEGADF DFLTASGANS
//
