(data stored in ACNUC7421 zone)

SWISSPROT: C6WF52_ACTMD

ID   C6WF52_ACTMD            Unreviewed;       598 AA.
AC   C6WF52;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_00572, ECO:0000256|SAAS:SAAS00382275};
DE            EC=2.3.3.13 {ECO:0000256|HAMAP-Rule:MF_00572, ECO:0000256|SAAS:SAAS00382275};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_00572};
GN   Name=leuA {ECO:0000256|HAMAP-Rule:MF_00572};
GN   OrderedLocusNames=Amir_0213 {ECO:0000313|EMBL:ACU34184.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34184.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34184.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(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_00572, ECO:0000256|SAAS:SAAS00085026}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC       (2S)-2-isopropylmalate + CoA. {ECO:0000256|HAMAP-Rule:MF_00572,
CC       ECO:0000256|SAAS:SAAS00382256}.
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_00572, ECO:0000256|SAAS:SAAS00510686}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00572}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00572,
CC       ECO:0000256|SAAS:SAAS00570107}.
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DR   EMBL; CP001630; ACU34184.1; -; Genomic_DNA.
DR   RefSeq; WP_012782847.1; NC_013093.1.
DR   ProteinModelPortal; C6WF52; -.
DR   STRING; 446462.Amir_0213; -.
DR   EnsemblBacteria; ACU34184; ACU34184; Amir_0213.
DR   KEGG; ami:Amir_0213; -.
DR   eggNOG; ENOG4107QXN; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000110941; -.
DR   KO; K01649; -.
DR   OMA; TWPDKVI; -.
DR   OrthoDB; POG091H01V5; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00572; LeuA_type2; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005668; IPM_Synthase.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR10277:SF53; PTHR10277:SF53; 1.
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; TIGR00970; leuA_yeast; 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; C6WF52.
DR   SWISS-2DPAGE; C6WF52.
KW   Acyltransferase {ECO:0000313|EMBL:ACU34184.1};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572,
KW   ECO:0000256|SAAS:SAAS00504085};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_00572, ECO:0000256|SAAS:SAAS00504087};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572,
KW   ECO:0000256|SAAS:SAAS00510687};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00572,
KW   ECO:0000256|SAAS:SAAS00108429, ECO:0000313|EMBL:ACU34184.1}.
FT   DOMAIN       69    343       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
SQ   SEQUENCE   598 AA;  66049 MW;  32F16BDE728D2702 CRC64;
     MSTISPDAYS TGTSRIRPPA RPAPEGQPAW NPQRGTSMPV HRYRPFHELV ETVDLPDRTW
     PAKRITQAPQ WCAVDLRDGN QALIDPMSPA RKRKMFDLLV RMGYKEIEVG FPAASQTDFD
     FVREIIEDGA VPDDVTIQVL TQCRPELITR TYESLRGAHK AIVHFYNSTS VLQRKVVFRA
     DRDRIKAIAT DAARFALEEA KKYPETEFRY EYSPESYTGT ELSYALEVCD AVSEIIAPTP
     ELPMVINLPA TVEMATPNVY ADSIEWMSRH LARRDSIVLS LHPHNDRGTG VAAAELGYLA
     GADRIEGCLF GNGERTGNVC LVTLGMNMFS QGVDPQIDFS DIDEVRRTVE YCNQLPVHER
     HPYGGDLVFT AFSGSHQDAI KKGFEALEAD AKDADKHVDE YPWEVPYLPI DPKDVGRNYE
     AVIRVNSQSG KGGVAYVMKS EHHLDLPRRL QVEFSRVIQE VTDTQGGEVG PKEIWDAFAD
     EYLQGVAPLR LLKHELSSDG TGSESIKTVL VVDGETQDVT GTGNGPIAAF VDALASVGYD
     VRVLDYSEHA LSSGDDARAA SYVECSVGDR VLWGVGVDSS TVAASLRALV SAVNRANR
//

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