ID   F6A8G7_PSEF1            Unreviewed;       215 AA.
AC   F6A8G7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
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            Short=IPMI {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=Psefu_3074 {ECO:0000313|EMBL:AEF23038.1};
OS   Pseudomonas fulva (strain 12-X).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF23038.1, ECO:0000313|Proteomes:UP000000686};
RN   [1] {ECO:0000313|EMBL:AEF23038.1, ECO:0000313|Proteomes:UP000000686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA   Woyke T.;
RT   "Complete sequence of Pseudomonas fulva 12-X.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|ARBA:ARBA00002695, ECO:0000256|HAMAP-Rule:MF_01031}.
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; Evidence={ECO:0000256|ARBA:ARBA00000491,
CC         ECO:0000256|HAMAP-Rule:MF_01031};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|ARBA:ARBA00004729,
CC       ECO:0000256|HAMAP-Rule:MF_01031}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|ARBA:ARBA00011271,
CC       ECO:0000256|HAMAP-Rule:MF_01031}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009845, ECO:0000256|HAMAP-Rule:MF_01031}.
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DR   EMBL; CP002727; AEF23038.1; -; Genomic_DNA.
DR   RefSeq; WP_013792165.1; NC_015556.1.
DR   AlphaFoldDB; F6A8G7; -.
DR   STRING; 743720.Psefu_3074; -.
DR   KEGG; pfv:Psefu_3074; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_0_3_6; -.
DR   OrthoDB; 9777465at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000686; Chromosome.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01577; IPMI_Swivel; 1.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR   HAMAP; MF_01031; LeuD_type1; 1.
DR   InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR033940; IPMI_Swivel.
DR   NCBIfam; TIGR00171; leuD; 1.
DR   PANTHER; PTHR43345:SF5; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT; 1.
DR   PANTHER; PTHR43345; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 2-RELATED-RELATED; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01031};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01031};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01031};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01031};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000686}.
FT   DOMAIN          1..132
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   215 AA;  24328 MW;  2B521DDBC18A2E28 CRC64;
     MKAFTQHTGL VCPLDRANVD TDQIIPKQFL KSIKRTGFGP NLFDEWRYLD VGQPNQDNSK
     RPINKDFVLN FPRYQGASVL LARENFGCGS SREHAPWALD EYGFRTVIAP SFADIFFNNS
     FKNGLLPIIL KAEEVDALFE QAEASEGYQL TVDLEAQTVT RPDGVQYSFE VDAFRKHCLL
     NGLDDIGLTL QDAEAIRAFE VGYQQRQPWL FGAVK
//