(data stored in ACNUC7421 zone)

SWISSPROT: A8FQ84_SHESH

ID   A8FQ84_SHESH            Unreviewed;       364 AA.
AC   A8FQ84;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE            EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01033};
DE   AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01033};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE            Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01033};
GN   Name=leuB {ECO:0000256|HAMAP-Rule:MF_01033};
GN   OrderedLocusNames=Ssed_0394 {ECO:0000313|EMBL:ABV35007.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35007.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35007.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35007.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2
CC       oxopentanoate. {ECO:0000256|HAMAP-Rule:MF_01033,
CC       ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571560}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-
CC         oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01033,
CC         ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS01118041};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00611795};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
CC       ECO:0000256|SAAS:SAAS00571573}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01033,
CC       ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571561}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01033}.
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DR   EMBL; CP000821; ABV35007.1; -; Genomic_DNA.
DR   RefSeq; WP_012140744.1; NC_009831.1.
DR   STRING; 425104.Ssed_0394; -.
DR   EnsemblBacteria; ABV35007; ABV35007; Ssed_0394.
DR   KEGG; sse:Ssed_0394; -.
DR   eggNOG; ENOG4105C0C; Bacteria.
DR   eggNOG; COG0473; LUCA.
DR   HOGENOM; HOG000021112; -.
DR   KO; K00052; -.
DR   OMA; EYDLGAR; -.
DR   OrthoDB; 1551125at2; -.
DR   BioCyc; SSED425104:G1G9Y-411-MONOMER; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   PANTHER; PTHR42979; PTHR42979; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00169; leuB; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQ84.
DR   SWISS-2DPAGE; A8FQ84.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571577};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
KW   ECO:0000256|SAAS:SAAS00571571};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571574};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571572};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571566};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571558};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
KW   ECO:0000256|SAAS:SAAS00571565};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571564, ECO:0000313|EMBL:ABV35007.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015}.
FT   DOMAIN        4    356       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      76     89       NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   NP_BIND     283    295       NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       225    225       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       249    249       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       253    253       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   BINDING      97     97       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     107    107       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     225    225       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   SITE        143    143       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   SITE        193    193       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
SQ   SEQUENCE   364 AA;  39290 MW;  61162B1571771457 CRC64;
     MSYQIAVLAG DGIGSEVMAE ARKVLSAVEE RFELAIEYSE YDIGGAAIDN HGCPLPEVTL
     KGCEAADAIL FGSVGGPKWE HLPPNDQPER GALLPLRGHF ELFCNMRPAK LHAGLEHMSP
     LRSDISGKGF DVLCVRELTG GIYFGKPKGR QGEGEEEEAF DTMRYSRKEI RRIAKIAFEA
     AQGRRKKVTS VDKANVLACS VLWREVVEEV AKDYPDVELE HIYIDNATMQ LLRRPDEFDV
     MLCSNLFGDI ISDEIAMLTG SMGLLSSVSM NSKGFGLYEP AGGSAPDIAG QGIANPVAQI
     LSAALLLRHS LKLESAAVAI EAAVGKALSD GYLTGELLPA SQRANAKSTS EMGDYITKLV
     KEGI
//

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