ID Q7ZAG6_HALVO Unreviewed; 202 AA.
AC Q7ZAG6;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00011998};
DE EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998};
GN Name=leuD {ECO:0000313|EMBL:CAE00174.1};
GN ORFNames=JK351_01985 {ECO:0000313|EMBL:MBS8117937.1}, JK352_01985
GN {ECO:0000313|EMBL:MBS8130683.1}, JK353_01985
GN {ECO:0000313|EMBL:MBS8126817.1}, JK354_01985
GN {ECO:0000313|EMBL:MBS8122949.1};
OS Haloferax volcanii (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=2246 {ECO:0000313|EMBL:CAE00174.1};
RN [1] {ECO:0000313|EMBL:CAE00174.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DS70 {ECO:0000313|EMBL:CAE00174.1};
RX PubMed=14766575; DOI=10.1128/AEM.70.2.943-953.2004;
RA Allers T., Ngo H.P., Mevarech M., Lloyd R.G.;
RT "Development of additional selectable markers for the halophilic archaeon
RT Haloferax volcanii based on the leuB and trpA genes.";
RL Appl. Environ. Microbiol. 70:943-953(2004).
RN [2] {ECO:0000313|EMBL:MBS8117937.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H98 {ECO:0000313|EMBL:MBS8117937.1}, ID112
RC - delta_ftsZ1_delta_ftsZ2 {ECO:0000313|EMBL:MBS8130683.1}, ID76
RC - delta_ftsZ1 {ECO:0000313|EMBL:MBS8122949.1}, and ID77 - delta_ftsZ2
RC {ECO:0000313|EMBL:MBS8126817.1};
RX PubMed=33903747; DOI=10.1038/s41564-021-00894-z;
RA Liao Y., Ithurbide S., Evenhuis C., Loewe J., Duggin I.G.;
RT "Cell division in the archaeon Haloferax volcanii relies on two FtsZ
RT proteins with distinct functions in division ring assembly and
RT constriction.";
RL Nat. Microbiol. 6:594-605(2021).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000256|ARBA:ARBA00002695}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004729}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|ARBA:ARBA00011271}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009845}.
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DR EMBL; AJ571689; CAE00174.1; -; Genomic_DNA.
DR EMBL; JAERQU010000001; MBS8117937.1; -; Genomic_DNA.
DR EMBL; JAERQV010000001; MBS8122949.1; -; Genomic_DNA.
DR EMBL; JAERQW010000001; MBS8126817.1; -; Genomic_DNA.
DR EMBL; JAERQX010000001; MBS8130683.1; -; Genomic_DNA.
DR RefSeq; WP_004043432.1; NZ_JAERQX010000001.1.
DR AlphaFoldDB; Q7ZAG6; -.
DR GeneID; 8926244; -.
DR OMA; MEAFTTH; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000676028; Unassembled WGS sequence.
DR Proteomes; UP000678484; Unassembled WGS sequence.
DR Proteomes; UP000679371; Unassembled WGS sequence.
DR Proteomes; UP000679789; Unassembled WGS sequence.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 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};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAE00174.1}.
FT DOMAIN 12..123
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 22013 MW; 54A75F4D78563D81 CRC64;
MTDEIPEIDS ASGTGVPIRG NDIDTDQIIP ARFMKVVTFD GLGEFAFFDQ RYDENDEPKD
HPLNEPQFQD ASIMVVNANF GCGSSREHAP QALMRWGIDA IVGESFAEIF AGNCLALGIP
TVTADHETVT ELQDWVDEHP DGDIDVDVEN ETVTYGDTTV DVTVDDAQRK ALTEGVWDTT
ALMKSNADAV AEKAAALPYV DD
//
