ID A0A2H3T9E4_FUSOX Unreviewed; 777 AA.
AC A0A2H3T9E4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00014371, ECO:0000256|PIRNR:PIRNR001418};
DE EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998, ECO:0000256|PIRNR:PIRNR001418};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|ARBA:ARBA00031631, ECO:0000256|PIRNR:PIRNR001418};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|ARBA:ARBA00033368, ECO:0000256|PIRNR:PIRNR001418};
GN ORFNames=BFJ68_g7301 {ECO:0000313|EMBL:RKL13312.1}, BFJ69_g7447
GN {ECO:0000313|EMBL:RKK75735.1}, FOXYS1_8968
GN {ECO:0000313|EMBL:KAF5260380.1}, FRV6_09485
GN {ECO:0000313|EMBL:SCO85358.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO85358.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SCO85358.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|EMBL:SCO85358.1};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000285084, ECO:0000313|Proteomes:UP000285860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo_A13 {ECO:0000313|EMBL:RKK75735.1,
RC ECO:0000313|Proteomes:UP000285084}, and Fo_A28
RC {ECO:0000313|EMBL:RKL13312.1, ECO:0000313|Proteomes:UP000285860};
RX PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT "Characterisation of pathogen-specific regions and novel effector
RT candidates in Fusarium oxysporum f. sp. cepae.";
RL Sci. Rep. 8:13530-13530(2018).
RN [4] {ECO:0000313|EMBL:KAF5260380.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 39464 {ECO:0000313|EMBL:KAF5260380.1};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000256|ARBA:ARBA00002695, ECO:0000256|PIRNR:PIRNR001418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33; Evidence={ECO:0000256|ARBA:ARBA00000491,
CC ECO:0000256|PIRNR:PIRNR001418};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|ARBA:ARBA00004729,
CC ECO:0000256|PIRNR:PIRNR001418}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|PIRNR:PIRNR001418}.
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DR EMBL; JAAFOW010001496; KAF5260380.1; -; Genomic_DNA.
DR EMBL; MRCX01000058; RKK75735.1; -; Genomic_DNA.
DR EMBL; MRCY01000030; RKL13312.1; -; Genomic_DNA.
DR EMBL; FMJY01000005; SCO85358.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOC1_g10011180; -.
DR VEuPathDB; FungiDB:FOC4_g10002477; -.
DR VEuPathDB; FungiDB:FOIG_05803; -.
DR VEuPathDB; FungiDB:FOMG_10560; -.
DR VEuPathDB; FungiDB:FOXG_06292; -.
DR VEuPathDB; FungiDB:FOZG_07273; -.
DR VEuPathDB; FungiDB:HZS61_012443; -.
DR OrthoDB; 1122834at2759; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR Proteomes; UP000285084; Unassembled WGS sequence.
DR Proteomes; UP000285860; Unassembled WGS sequence.
DR Proteomes; UP000558688; Unassembled WGS sequence.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01583; IPMI; 1.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR HAMAP; MF_01026; LeuC_type1; 1.
DR HAMAP; MF_01031; LeuD_type1; 1.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR InterPro; IPR012235; 3-IsopropMal_deHydtase_ssu/lsu.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR033940; IPMI_Swivel.
DR NCBIfam; TIGR00170; leuC; 1.
DR NCBIfam; TIGR00171; leuD; 1.
DR PANTHER; PTHR43822:SF9; 3-ISOPROPYLMALATE DEHYDRATASE; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PIRSF; PIRSF001418; ACN; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR001418};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|PIRNR:PIRNR001418}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430,
KW ECO:0000256|PIRNR:PIRNR001418};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001418};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000558688}.
FT DOMAIN 13..472
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 540..662
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 488..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 84839 MW; A41E04385C71CAAE CRC64;
MPAPVGNPQT LYDKVFSAHI VDEKLDGTIL LYIDRHLVHE VTSPQAFEGL ENAGRKVRRP
DCTLATTDHN VPTTSRKALK DIASFIEEDD SRTQCVTLEE NVKKFGVTYF GLGDKRQGIV
HIIGPEQGFT LPGTTVVCGD SHTSTHGAFG ALAFGIGTSE VEHVLATQCL ITKRSKNMRI
QIDGELAPGV SSKDVVLHAI GRIGTAGGTG AVIEFCGSVI RNLSMEARMS ICNMSIEGGA
RAGMVAPDEI TFEYLKGRPL APKYGSETWN QAVAYWKSLQ SDPGAKYDID VFIDAKDIIP
TITWGTSPED VVPITGCVPD PETFSSESKK AAGRRMLEYM GLTAGTPMED IPVDKVFIGS
CTNARIEDLR AAANVVKGRK VADNIRRAMV VPGSGLVKAQ AEEEGLDQIF VDAGFEWREA
GCSMCLGMNP DILAPKERCA STSNRNFEGR QGALSRTHLM SPVMAAAAAI VGKLADVRKL
SHYTHQSAFK PRELPAEEPH VDERTRDDSE EREMIGDQPQ DSQPHTNTLA SAGGAASGLP
KFTIWKGTAA PLDRSNVDTD AIIPKQFLKT IKRTGLGTAL FYELRYKEDG SENPDFVLNQ
EPFRQAKTLV VTGPNFGCGS SREHAPWALL DFGIKCIIAP SFADIFFNNT FKNGMLPIRI
EDKDNLEAIA AEARANRDIE IDLPNQLIKN ADGETICSFD VEEFRKHCLV NGLDDIGLTM
QQEDKIAEFE RRMTQNTPWL DGTGYLKRPG QGGKLAAKAV PVPKTNRGEE KKEPLEW
//
