(data stored in SCRATCH zone)

SWISSPROT: Q5LWC0_RUEPO

ID   Q5LWC0_RUEPO            Unreviewed;       524 AA.
AC   Q5LWC0;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 104.
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   ECO:0000313|EMBL:AAV93740.1};
GN   OrderedLocusNames=SPO0422 {ECO:0000313|EMBL:AAV93740.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93740.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93740.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93740.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93740.1; -; Genomic_DNA.
DR   RefSeq; WP_011046183.1; NC_003911.12.
DR   STRING; 246200.SPO0422; -.
DR   EnsemblBacteria; AAV93740; AAV93740; SPO0422.
DR   KEGG; sil:SPO0422; -.
DR   eggNOG; ENOG4105CYQ; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000046859; -.
DR   KO; K01649; -.
DR   OMA; NDTGMAI; -.
DR   OrthoDB; 840579at2; -.
DR   BioCyc; RPOM246200:G1G48-429-MONOMER; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001023; 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; Q5LWC0.
DR   SWISS-2DPAGE; Q5LWC0.
KW   Acyltransferase {ECO:0000313|EMBL:AAV93740.1};
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:UP000001023};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01025,
KW   ECO:0000256|SAAS:SAAS00459347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01025,
KW   ECO:0000256|SAAS:SAAS00131367, ECO:0000313|EMBL:AAV93740.1}.
FT   DOMAIN       10    271       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
SQ   SEQUENCE   524 AA;  57156 MW;  739DEBDB76E5846A CRC64;
     MTHVTDQDRV LIFDTTLRDG EQSPGATMTH TEKLEIAEML DEMGVDIIEA GFPIASEGDF
     KAVSEIAKRA QNSRICGLAR ANFADIDRCW EAVKHAEKNR IHTFIGTSPL HRAIPNLTQD
     EMAEKIHETV SHARNLCDNV QWSPMDATRT EWDYLCRVIE IAIKAGATTI NIPDTVGYTA
     PAESADLIRR LIETVPGADD VIFATHCHND LGMATANSLA AVAGGARQIE CTINGLGERA
     GNTALEEVVM AMKTRHDIMP WRTGIDTTKI MAISRRVATV SGFNVQFNKA IVGKNAFAHE
     SGIHQDGMLK NRENFEIMRP EDIGLSGTSL PLGKHSGRAA LRDKLEHLGY EVGDNQLKDI
     FVRFKELADR KKEVFDDDVI ALMRSGENAE QDHLQLVSMK VICGTGGPAE ATVEMEIDGK
     DVSATAHGDG PVDASFKAIR ALHPNEAHLQ LYQVHAVTEG TDAQATVSVR LEEDGMIATG
     ESANTDTVVA SAKAYINALN RLIVRREKAG PGADAREISY KDLT
//

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