ID   Q5B0P4_EMENI            Unreviewed;       772 AA.
AC   Q5B0P4; C8UZW6;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 118.
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=ANIA_05886 {ECO:0000313|EMBL:CBF70635.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF70635.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA   Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA   Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; BN001301; CBF70635.1; -; Genomic_DNA.
DR   RefSeq; XP_663490.1; XM_658398.1.
DR   AlphaFoldDB; Q5B0P4; -.
DR   STRING; 227321.Q5B0P4; -.
DR   EnsemblFungi; CBF70635; CBF70635; ANIA_05886.
DR   GeneID; 2870766; -.
DR   KEGG; ani:AN5886.2; -.
DR   VEuPathDB; FungiDB:AN5886; -.
DR   eggNOG; KOG0454; Eukaryota.
DR   HOGENOM; CLU_006714_0_0_1; -.
DR   InParanoid; Q5B0P4; -.
DR   OMA; EDNEPHT; -.
DR   OrthoDB; 1122834at2759; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000560; Chromosome I.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097308; P:cellular response to farnesol; IEP:AspGD.
DR   GO; GO:0009098; P:leucine biosynthetic process; IMP:AspGD.
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   Isomerase {ECO:0000313|EMBL:CBF70635.1};
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:UP000000560}.
FT   DOMAIN          13..472
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          536..657
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   REGION          489..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   772 AA;  84105 MW;  06E769007FB6BD14 CRC64;
     MPGADRKPKT LYDKVFDHHI VNEQEDGTVL IYIDRHLVHE VTSPQAFEGL KNANRKVRRP
     DCTLVTVDHN IPTSSRKNFK NVEQFIEEND SRLQCSTLEE NVKDFGLTYF GMDDKRQGIV
     HVIGPEQGFT LPGTTVVCGD SHTSTHGAFG ALAFGIGTSE VEHVLATQTL ITRRSKNMRV
     QVDGELPAGV TSKDVVLHII GLIGTAGGTG CVIEFCGSVI RGLSMEARMS MCNMSIEGGA
     RAGMVAPDET TFEYLKGRPL APKYDSAEWK KAVSYWSSLA SDEDAVYDKT ILIDAKDIVP
     TISWGTSPQD VVPITGVVPG PDDFEDEARK AACKRALEYM GLTAGTPMKD VTVDKVFIGS
     CTNSRIEDLR AAANVVRGKK VASNIKRAMV VPGSGLVKQQ AEAEGLDKIF IDAGFEWREA
     GCSMCLGMNP DILSPQERCA STSNRNFEGR QGAGGRTHLM SPAMAAAAAI VGKLADVREH
     IAESPRLGKV QPKVDVKPEA EDVDTEEELD HILDQPADNE PHTNTHTPAT TSAGLPKFTT
     LKGIAAPMDR SNVDTDAIIP KQFLKTIKRT GLGSALFYEL RYKDGQEDPS FILNQGIYRN
     SKILVVTGPN FGCGSSREHA PWALLDFGIK CVIAPSFADI FFNNTFKNGM LPVVIPDQAV
     LEKIADEARA GREVEVDLVN QEIKDEAGNK LASFDVDAFR KHCLINGLDD IGLTLQMEDK
     IAKFEAKRTL DTPWLDGKAY LKRGRTGGSN MVKAAPVPKT NRGDVKGEPL EW
//