LEU11_HYDCU
ID LEU11_HYDCU Reviewed; 514 AA.
AC Q31I16;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=2-isopropylmalate synthase 1 {ECO:0000255|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-IPM synthase 1 {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase 1 {ECO:0000255|HAMAP-Rule:MF_01025};
GN Name=leuA1 {ECO:0000255|HAMAP-Rule:MF_01025}; OrderedLocusNames=Tcr_0611;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000255|HAMAP-
CC Rule:MF_01025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01025};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000255|HAMAP-
CC Rule:MF_01025}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000109; ABB41207.1; -; Genomic_DNA.
DR RefSeq; WP_011370032.1; NC_007520.2.
DR AlphaFoldDB; Q31I16; -.
DR SMR; Q31I16; -.
DR STRING; 317025.Tcr_0611; -.
DR EnsemblBacteria; ABB41207; ABB41207; Tcr_0611.
DR KEGG; tcx:Tcr_0611; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_6; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR HAMAP; MF_01025; LeuA_type1; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 1.
DR TIGRFAMs; TIGR00973; leuA_bact; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Transferase.
FT CHAIN 1..514
FT /note="2-isopropylmalate synthase 1"
FT /id="PRO_1000149322"
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 514 AA; 55848 MW; C929085BC6024F2A CRC64;
MKEELVIFDT TLRDGEQSPG ASMTKEEKVR IAKQLEKLRV NVIEAGFPAA SQGDFESVQA
VASAVKDSTV CGLARAVEND IVRAGEAIKL ANSGRIHTFI ATSPIHMEKK LKMSPDEVVE
RAVWAVKRAR DFTDNVEFSP EDAGRSELDF LCRVIEAAID AGATTINIPD TVGYNVPEQF
GELFHQLLNR IPNADKAIFS AHCHNDLGLA VANSLAAVKS GARQVECTIN GLGERAGNTA
LEEVVMAVRT RQDWFDVDTR IHTPEILAAS RLVAGITGFA VQPNKAIVGT NAFSHESGIH
QDGVLKHRET YEIMRAEDVG WSTNKMVLGK HSGRSAFRSR LKELGIEFET EQELSDAFIS
FKELADRKHE IYDEDIQALV TDNNTRRVEN ETFRLVALKV GTQTGDAPTA TITLWIDGEE
KTASSEGGGV VDATFKAIEK LVDSGATLEL YSVSNVTNGT DSLGETTVRM EKAGRIVNGQ
GADTDIVTAS AKAYINALNK LIDTGSKEHP QAHV