ID LEUC_SULAC Reviewed; 414 AA.
AC Q4JC09;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=3-isopropylmalate dehydratase large subunit;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE Short=IPMI;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leuC; OrderedLocusNames=Saci_0253;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 /
OS NBRC 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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 isopropylmalate.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD (By similarity).
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC type 2 subfamily.
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DR EMBL; CP000077; AAY79670.1; -; Genomic_DNA.
DR RefSeq; YP_254963.1; NC_007181.1.
DR STRING; 330779.Saci_0253; -.
DR EnsemblBacteria; AAY79670; AAY79670; Saci_0253.
DR GeneID; 3474810; -.
DR KEGG; sai:Saci_0253; -.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226971; -.
DR KO; K01703; -.
DR OMA; ANGVCHA; -.
DR ProtClustDB; PRK00402; -.
DR BioCyc; SACI330779:GH9J-329-MONOMER; -.
DR UniPathway; UPA00048; UER00071.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:HAMAP.
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:HAMAP.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
DR HAMAP; MF_01027; LeuC_type2; 1; -.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR015937; Acoase/IPM_deHydtase.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR PANTHER; PTHR11670:SF6; PTHR11670:SF6; 1.
DR Pfam; PF00330; Aconitase; 2.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase_N; 1.
DR TIGRFAMs; TIGR01343; hacA_fam; 1.
DR TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding.
FT CHAIN 1 414 3-isopropylmalate dehydratase large
FT subunit.
FT /FTId=PRO_0000076884.
FT METAL 297 297 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 355 355 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 358 358 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 414 AA; 44616 MW; 3CC33E8DA192CD1B CRC64;
MPQTLTEKIL SRASGKNVSP GDVTEIKVDL VAFHDLTGYH VIEVMEDVGT LKVFDREKLV
IAFDHLAPPP DVRSAEIQGQ IRNFVKKTSV PNFYDINSGI LHQIMIERYA NPGQVIVAAD
SHTSTSGAVG AFAQGLGASD VAAAVITGKT WVMVPQPFKI TLEGKPARWI NGKDIALKIL
GDFKADYFNG MSLEIFVKEP SAVPMDFRAT VSNMGIEMNA DALMFVPDQE TFNYIKTARG
YEPQMVTPDS DAKYVDEYNI DLSKLDPLVA APHSVDNVKS VNEVEGTPVD QVFIGSCTNG
RISDLEMAAK ILKGKKVKTR TIVIPASYQL FKKALELGYV QTLADAGAII TYGTCGPCLG
GHFGIAGPGE TIISTSSRNF KGRMGSPDAK VYLSGPAVAA ATALEGKITD PRRL
//
