ID A0A1J7IXA0_9PEZI Unreviewed; 690 AA.
AC A0A1J7IXA0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3-isopropylmalate dehydratase {ECO:0000313|EMBL:OIW25705.1};
GN ORFNames=CONLIGDRAFT_708439 {ECO:0000313|EMBL:OIW25705.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW25705.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW25705.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW25705.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV875101; OIW25705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7IXA0; -.
DR STRING; 1408157.A0A1J7IXA0; -.
DR InParanoid; A0A1J7IXA0; -.
DR OrthoDB; 1326656at2759; -.
DR Proteomes; UP000182658; 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 GO; GO:1901607; P:alpha-amino acid biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR NCBIfam; TIGR02087; LEUD_arch; 1.
DR PANTHER; PTHR43822:SF2; 3-ISOPROPYLMALATE DEHYDRATASE LARGE SUBUNIT, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 2.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 4: Predicted;
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:UP000182658}.
FT DOMAIN 92..307
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 313..432
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 545..600
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 669..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 74886 MW; AE898AAAA8E3E5B4 CRC64;
MADATAQETG LNACEKVLIH HAVGLSSTPS YIPTDQVLLL KPSWLLCSEA AWNSMEPNYN
ALGRPSFRRK DRFWLAPDHM VDPRVNHRPR EKAIIEKCER IARDMNLGDN YNPPNTTIMH
TDFYRKRCQP GQLVVGADSH TGSAGSLGAL AIGMGITDVL MQVVTGETFL KMPEVICIRL
VGRPPLGLGG KDVIMGVLGQ LKRNTVAAER LVEFVGEGLR WLSCDARFAI CNMVTELGGI
GALVVPDAVT AEYIARRPER RHKSDAVFFK PDANARYAGE YKIDLSELEH CVALYPSPDN
VVPVSQAELP ELQGCFIGAC TTTEEDLILA GLVLREGLKA GLRPVSRGLR RVTPGSVDIT
EKLRRLGLID VYQEAGFTVG APGCSYCVGM GIDKAGRGEV WLSSQNRNYR DRMGPGSIAN
LASAATVAAS SFSMTLQSPQ QLLDQIDFTE YDRLREYYSP SMDQVADPTY SEPSPVMPPS
QAQQESVISS LPSLICGRIQ RFGDNVDTDS IAPTEICLGS PTPEALARGA FCHTRPEFHE
RARAGATVVV AGTAFGTGSS REQAPKVLLA AGIQAVVARS FAFIYGRNQA NSGLLGVKVR
DDRFYELAGE GVEVEIDVEG RVVVCGGERF GFRLDAIEER LIAAGGLLKM YDLHGNALFQ
YLQDAVSTGT GPTDGTVDRA ETRGDGRLEW
//