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LEUD1_DEIRA
ID   LEUD1_DEIRA             Reviewed;         177 AA.
AC   Q9RTY5;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit 1;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase 1;
DE            Short=IPMI 1;
DE   AltName: Full=Isopropylmalate isomerase 1;
GN   Name=leuD1; OrderedLocusNames=DR_1614;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC         Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC         EC=4.2.1.33;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000513; AAF11175.1; -; Genomic_DNA.
DR   PIR; H75373; H75373.
DR   RefSeq; NP_295337.1; NC_001263.1.
DR   RefSeq; WP_010888252.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RTY5; -.
DR   SMR; Q9RTY5; -.
DR   STRING; 243230.DR_1614; -.
DR   EnsemblBacteria; AAF11175; AAF11175; DR_1614.
DR   KEGG; dra:DR_1614; -.
DR   PATRIC; fig|243230.17.peg.1819; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_1_1_0; -.
DR   InParanoid; Q9RTY5; -.
DR   OMA; APFMVGE; -.
DR   OrthoDB; 1384217at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01032; LeuD_type2; 1.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   TIGRFAMs; TIGR02087; LEUD_arch; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..177
FT                   /note="3-isopropylmalate dehydratase small subunit 1"
FT                   /id="PRO_0000141923"
FT   REGION          157..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   177 AA;  19440 MW;  03718FA8359B553B CRC64;
     MPRIWKFGDS VNTDDILPGK FAPFMAGEDV FQTFAFHYVR PEFAAQVQPG DVLIGGRNWG
     LGSSREYAPQ ALKKLHIGGI VAPSFARIHY RNLLNLGIPA FEYDLTELLE DGDEVTLDAQ
     TGLLTYADGT VQLPPPPEFL REALKEGSIL EFFKKHGRFP GEEPGAEAST ETASAAE
 
 
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