ID   Q9HLW3      PRELIMINARY;      PRT;   869 AA.
AC   Q9HLW3;
DT   01-MAR-2001 (TrEMBLrel. 16, Created)
DT   01-MAR-2001 (TrEMBLrel. 16, Last sequence update)
DT   01-MAR-2004 (TrEMBLrel. 26, Last annotation update)
DE   Probable aconitate hydratase.
GN   OrderedLocusNames=Ta0112;
OS   Thermoplasma acidophilum.
OC   Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=2303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1728;
RX   MEDLINE=20479972; PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmaleate + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (2S)-2-isopropylmaleate + H(2)O = 3-hydroxy-4-
CC       methyl-3-carboxypentanoate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- PATHWAY: Leucine biosynthesis; second step.
CC   -!- SUBUNIT: Heterodimer of leuC and leuD (By similarity).
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DR   EMBL; AL445063; CAC11259.1; -.
DR   HSSP; P16276; 1B0J.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA.
DR   GO; GO:0005506; F:iron ion binding; IEA.
DR   GO; GO:0016829; F:lyase activity; IEA.
DR   GO; GO:0003723; F:RNA binding; IEA.
DR   GO; GO:0008152; P:metabolism; IEA.
DR   InterPro; IPR006249; Aconitase_1.
DR   InterPro; IPR000573; Aconitase_C.
DR   InterPro; IPR001030; Aconitase_N.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   ProDom; PD000511; Aconitase_N; 1.
DR   TIGRFAMs; TIGR01341; aconitase_1; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
KW   4Fe-4S; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Leucine biosynthesis; Metal-binding.
SQ   SEQUENCE   869 AA;  96342 MW;  832C3FFB59338520 CRC64;
     MNGKKVYYYP LRKIFGEKVN SLPRSLRIIL ESMVRNLDGR SISDSDINAI LNWNAENVAD
     TEIRFKVSRV VMQDFTGVPA VVDLASMRDT VKNLGKDPEL INPQVRVDLV IDHSVQVDYY
     GETFALEKNE ELEFDRNMER YRFLKWAQKA FKNFKVIPPG TGIIHQVNLE YLAEVVFEGK
     KDGKDYAYFD SLVGTDSHTT MINGIGVLGW GVGGIEAEAA LLGQPITISL PEVIGVRIKG
     KMQPGVTATD VVLTVTEMLR KVNVVDKFVE FFGPSVKYLS VPERATISNM CPEFGATCAL
     FPIDDQTLQY LETTGRPKDH IDLIKKYLEA QGLFGEGAEP KYTRVIELDL STVKPSVAGP
     KLPQQRLDLD QVPASFLSTL EQNGGDRLVT LRKVPLKMKG QNLELSDGDI VIAAITSCTN
     TSNPYVMIAA GLLAKKAVEA GLKVNPKVKT SLAPGSRVVT DYLTESGLLS YLEKLGFYIV
     GYGCTTCIGN SGPLDQDLGN AIVNNNLSVV SVLSGNRNFE ARIHKDVKAN YLMSPPLVVA
     YALAGNITVN LNKDPIATVG GKKVYLKDIW PTNEEINEAV NKYVRKDMFE KRYGNITNER
     WEKIDAPSSP TYAWDPKSTY IRNPPFFENF RLDQEFTDFR IKGAYPLLVL GDSITTDHIS
     PAGSIAKDSP AAKYLIENGV KPEDFNSYGS RRGNHEVMMR GTFANVRIKN LMVKREGGYT
     LFVPENKEMS VYDAAMQYKK MGIPVVVIAG KEYGTGSSRD WAAKGTYLLG VKAVIAKSYE
     RIHRSNLVGM GVIPIEYEGF NPQDIDYTKT IDVDIGSIDP GSKAKITYTD KKGEKHTIDV
     RLRVDTPAES DYIKSGGILQ YSLKKILAS
//