ID Q1Q105_KUEST Unreviewed; 162 AA.
AC Q1Q105;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 ECO:0000313|EMBL:CAJ73689.1};
GN ORFNames=KsCSTR_13400 {ECO:0000313|EMBL:QII10719.1}, KSMBR1_2773
GN {ECO:0000313|EMBL:SOH05260.1}, kuste2936
GN {ECO:0000313|EMBL:CAJ73689.1};
OS Kuenenia stuttgartiensis.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Kuenenia.
OX NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ73689.1};
RN [1] {ECO:0000313|EMBL:CAJ73689.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16598256; DOI=10.1038/nature04647;
RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., Taylor M.W.,
RA Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N.,
RA Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A.,
RA Snel B., Dutilh B.E., OpDenCamp H.J.M., vanDerDrift C., Cirpus I.,
RA vanDePas-Schoonen K.T., Harhangi H.R., vanNiftrik L., Schmid M.,
RA Keltjens J., vanDeVossenberg J., Kartal B., Meier H., Frishman D.,
RA Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M.,
RA LePaslier D.;
RT "Deciphering the evolution and metabolism of an anammox bacterium from a
RT community genome.";
RL Nature 440:790-794(2006).
RN [2] {ECO:0000313|EMBL:CAJ73689.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000221734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Frank J.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:SOH05260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH05260.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QII10719.1, ECO:0000313|Proteomes:UP000501926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSTR1 {ECO:0000313|EMBL:QII10719.1,
RC ECO:0000313|Proteomes:UP000501926};
RA Ding C., Adrian L.;
RT "Newly sequenced genome of strain CSTR1 showed variability in Candidatus
RT Kuenenia stuttgartiensis genomes.";
RL Submitted (FEB-2020) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT573071; CAJ73689.1; -; Genomic_DNA.
DR EMBL; CP049055; QII10719.1; -; Genomic_DNA.
DR EMBL; LT934425; SOH05260.1; -; Genomic_DNA.
DR KEGG; kst:KSMBR1_2773; -.
DR OrthoDB; 9777465at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
DR Proteomes; UP000501926; 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; IPR011824; LeuD/DmdB_bac.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR NCBIfam; TIGR02084; leud; 1.
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:UP000221734}.
FT DOMAIN 42..104
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 162 AA; 18192 MW; 3F42D4E8B209EB87 CRC64;
MKNKCWKFGN NINTDEIIPA RYLNTTDPNE LAKHCMEDAD PDFIKKIKQG DVIVAGENFG
CGSSREHAPI AIKAAGISCV IAKSFARIFF RNAINIGLLI FECPEAADNI KEGDEIEVDL
TKSEIFDHTL NRRFTFEPFP HEMQEIIQSG GLMNFVKNKI GQ
//
