(data stored in SCRATCH zone)

SWISSPROT: C8W660_DESAS

ID   C8W660_DESAS            Unreviewed;       532 AA.
AC   C8W660;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025, ECO:0000256|SAAS:SAAS00362855};
DE            EC=2.3.3.13 {ECO:0000256|HAMAP-Rule:MF_01025, ECO:0000256|SAAS:SAAS00085331};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025};
GN   Name=leuA {ECO:0000256|HAMAP-Rule:MF_01025};
GN   OrderedLocusNames=Dtox_0595 {ECO:0000313|EMBL:ACV61515.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61515.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61515.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of
CC       acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form
CC       3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
CC       {ECO:0000256|HAMAP-Rule:MF_01025, ECO:0000256|SAAS:SAAS00570112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524,
CC         ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
CC         EC=2.3.3.13; Evidence={ECO:0000256|HAMAP-Rule:MF_01025,
CC         ECO:0000256|SAAS:SAAS01124331};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01025, ECO:0000256|SAAS:SAAS00085321}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01025,
CC       ECO:0000256|SAAS:SAAS00362821}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01025,
CC       ECO:0000256|SAAS:SAAS00570119}.
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DR   EMBL; CP001720; ACV61515.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0595; -.
DR   EnsemblBacteria; ACV61515; ACV61515; Dtox_0595.
DR   KEGG; dae:Dtox_0595; -.
DR   eggNOG; ENOG4105CYQ; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000046859; -.
DR   KO; K01649; -.
DR   OMA; NDTGMAI; -.
DR   BioCyc; DACE485916:G1GFV-601-MONOMER; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002217; Chromosome.
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   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;
DR   PRODOM; C8W660.
DR   SWISS-2DPAGE; C8W660.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01025,
KW   ECO:0000256|SAAS:SAAS00161459};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01025, ECO:0000256|SAAS:SAAS00160591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01025,
KW   ECO:0000256|SAAS:SAAS00459347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01025,
KW   ECO:0000256|SAAS:SAAS00131367}.
FT   DOMAIN       28    290       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
SQ   SEQUENCE   532 AA;  58253 MW;  17EA6D04DC7E6245 CRC64;
     MSQQPTIIDD VQESDGSARV SSTNSRRVYI FDTTLRDGEQ SPGVSLNLSE KIQIARQLAL
     LGVDIIEAGF PIASTGDFEA VRGIAREVRG VAVAGLARAN FKDIDRAWEA LKEAEQPRIH
     TFLATSPIHM RYKLQMEPDK VLEMAVEAVK YAKKFTSDVE FSAEDGSRSD LDFLSRVVEA
     VIKAGATTVN IPDTVGYAMP QEYGNFIRSL MERVPNIDQA VVSVHCHNDL GLAVANSLAA
     VQNGVRQVEG AINGIGERAG NAAIEEIVMA LRTRKDFIGL NTNINTEEIY RTSKLVSKLT
     GMIVQANKAI VGKNAFAHES GIHQDGVLKE RSTYEIMNPA MIGINQDNLV LGKHSGRHAF
     RKRLGDLGYE LSEAELNKAF VRFKDLADKK KNITDRDLEA IVEEETRSHV PVKYIMEYFN
     ITSGSTIKPM AMVGLLSNDL LLQDTAFGDG PVDAIYKAID KIAGINCTLL HYSLDAITGG
     RDAQGDVTVK ISNEKGKSFI GRGVSTDILE ASAKAYVDAV NKLVYEADRR EE
//

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