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Database: UniProt
Entry: R4KKF3_9FIRM
LinkDB: R4KKF3_9FIRM
Original site: R4KKF3_9FIRM 
ID   R4KKF3_9FIRM            Unreviewed;       164 AA.
AC   R4KKF3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000256|HAMAP-Rule:MF_01032};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01032};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01032};
DE            Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01032};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01032};
GN   Name=leuD {ECO:0000256|HAMAP-Rule:MF_01032};
GN   ORFNames=Desgi_2646 {ECO:0000313|EMBL:AGL02052.1};
OS   Desulfoscipio gibsoniae DSM 7213.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL02052.1, ECO:0000313|Proteomes:UP000013520};
RN   [1] {ECO:0000313|EMBL:AGL02052.1, ECO:0000313|Proteomes:UP000013520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL02052.1,
RC   ECO:0000313|Proteomes:UP000013520};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA   Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA   Brambilla E., Spring S., Stams A.F., Woyke T.;
RT   "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL   Submitted (JAN-2012) 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|HAMAP-Rule:MF_01032}.
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|HAMAP-Rule:MF_01032};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01032}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01032}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009869, ECO:0000256|HAMAP-Rule:MF_01032}.
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DR   EMBL; CP003273; AGL02052.1; -; Genomic_DNA.
DR   RefSeq; WP_006521780.1; NC_021184.1.
DR   AlphaFoldDB; R4KKF3; -.
DR   STRING; 767817.Desgi_2646; -.
DR   KEGG; dgi:Desgi_2646; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_1_1_9; -.
DR   OrthoDB; 9777465at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000013520; Chromosome.
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_01032; LeuD_type2; 1.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR033940; IPMI_Swivel.
DR   InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR   NCBIfam; TIGR02087; LEUD_arch; 1.
DR   PANTHER; PTHR43345:SF2; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 1-RELATED; 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|HAMAP-Rule:MF_01032};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01032};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01032};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013520}.
FT   DOMAIN          50..99
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   164 AA;  17598 MW;  0DAC1F22B7BDA2B6 CRC64;
     MLKGRVCKFG ANIDTDAIIP ARYANLSDAV ELGKHCMENI EPGFSGRVKP GDILVAESNF
     GCGSSREIAP MAIMGAGISC VIARSFARIF FRNAINIGLP LLDCPEAIDK TKEGDYLEVD
     LSSGLIKNVT AGLLFKAVPF PSFIRDLISA GGLLEYTLKK DRGE
//
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