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Database: UniProt/TrEMBL
Entry: C7RRS8_ACCPU
LinkDB: C7RRS8_ACCPU
Original site: C7RRS8_ACCPU 
ID   C7RRS8_ACCPU            Unreviewed;       213 AA.
AC   C7RRS8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   29-OCT-2014, entry version 34.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000256|HAMAP-Rule:MF_01031};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01031};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01031};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01031};
GN   Name=leuD {ECO:0000256|HAMAP-Rule:MF_01031};
GN   OrderedLocusNames=CAP2UW1_1239 {ECO:0000313|EMBL:ACV34567.1};
OS   Accumulibacter phosphatis (strain UW-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria;
OC   Candidatus Accumulibacter.
OX   NCBI_TaxID=522306 {ECO:0000313|EMBL:ACV34567.1, ECO:0000313|Proteomes:UP000001619};
RN   [1] {ECO:0000313|EMBL:ACV34567.1, ECO:0000313|Proteomes:UP000001619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UW-1 {ECO:0000313|EMBL:ACV34567.1,
RC   ECO:0000313|Proteomes:UP000001619};
RG   US DOE Joint Genome Institute;
RA   Martin H.G., Ivanova N., Kunin V., Warnecke F., Barry K., He S.,
RA   Salamov A., Szeto E., Dalin E., Pangilinan J.L., Lapidus A., Lowry S.,
RA   Kyrpides N.C., McMahon K.D., Hugenholtz P.;
RT   "Complete sequence of chromosome of Candidatus Accumulibacter
RT   phosphatis clade IIA str. UW-1.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|HAMAP-Rule:MF_01031, ECO:0000256|SAAS:SAAS00135499}.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmalate. {ECO:0000256|HAMAP-Rule:MF_01031,
CC       ECO:0000256|SAAS:SAAS00089865}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01031, ECO:0000256|SAAS:SAAS00089854}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01031, ECO:0000256|SAAS:SAAS00135485}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01031}.
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DR   EMBL; CP001715; ACV34567.1; -; Genomic_DNA.
DR   RefSeq; YP_003166496.1; NC_013194.1.
DR   ProteinModelPortal; C7RRS8; -.
DR   STRING; 522306.CAP2UW1_1239; -.
DR   EnsemblBacteria; ACV34567; ACV34567; CAP2UW1_1239.
DR   GeneID; 8403376; -.
DR   KEGG; app:CAP2UW1_1239; -.
DR   PATRIC; 21258510; VBICanAcc132554_1516.
DR   eggNOG; COG0066; -.
DR   HOGENOM; HOG000222939; -.
DR   KO; K01704; -.
DR   OrthoDB; EOG661HCP; -.
DR   BioCyc; APHO522306:GHXL-1248-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01031; LeuD_type1; 1.
DR   InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR   InterPro; IPR015937; Acoase/IPM_deHydtase.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   SUPFAM; SSF52016; SSF52016; 1.
DR   TIGRFAMs; TIGR00171; leuD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01031,
KW   ECO:0000256|SAAS:SAAS00089858};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01031, ECO:0000256|SAAS:SAAS00089846};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001619};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01031,
KW   ECO:0000256|SAAS:SAAS00089867};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01031,
KW   ECO:0000256|SAAS:SAAS00089862};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001619}.
SQ   SEQUENCE   213 AA;  23765 MW;  849973D6F7C82B9C CRC64;
     MKPFTTLQGL VAPLDRANVD TDAIIPKQFL KSIKRSGFGP NAFDEWRYLD RGEPDRDCAT
     RPLNPDFVLN QPRYQGASIL LTRENFGCGS SREHAPWALE DYGFRAIIAP SFADIFFNNC
     FKNGILPIVL AATTVDRLFQ ETAAHAGYSL SLDLAAQTVT TPAGEVIPFV VDGECKHRLF
     NGLDDIGLTL LHTDKIKAYE ARRQAEAQWL FQT
//
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