ID V5WJS9_9SPIO Unreviewed; 476 AA.
AC V5WJS9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01026};
DE EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01026};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
DE Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01026};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
GN Name=leuC {ECO:0000256|HAMAP-Rule:MF_01026};
GN ORFNames=L21SP2_2695 {ECO:0000313|EMBL:AHC16047.1};
OS Salinispira pacifica.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Salinispira.
OX NCBI_TaxID=1307761 {ECO:0000313|EMBL:AHC16047.1, ECO:0000313|Proteomes:UP000018680};
RN [1] {ECO:0000313|EMBL:AHC16047.1, ECO:0000313|Proteomes:UP000018680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-RPul-D2 {ECO:0000313|EMBL:AHC16047.1,
RC ECO:0000313|Proteomes:UP000018680};
RX PubMed=26203324; DOI=10.1186/1944-3277-10-7;
RA Ben Hania W., Joseph M., Schumann P., Bunk B., Fiebig A., Sproer C.,
RA Klenk H.P., Fardeau M.L., Spring S.;
RT "Complete genome sequence and description of Salinispira pacifica gen.
RT nov., sp. nov., a novel spirochaete isolated form a hypersaline microbial
RT mat.";
RL Stand. Genomic Sci. 10:7-7(2015).
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_01026}.
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_01026};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01026};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01026};
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_01026}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC Rule:MF_01026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01026}.
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DR EMBL; CP006939; AHC16047.1; -; Genomic_DNA.
DR RefSeq; WP_024268945.1; NC_023035.1.
DR AlphaFoldDB; V5WJS9; -.
DR STRING; 1307761.L21SP2_2695; -.
DR KEGG; slr:L21SP2_2695; -.
DR PATRIC; fig|1307761.3.peg.2685; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_12; -.
DR OrthoDB; 9802769at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000018680; Chromosome.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR HAMAP; MF_01026; LeuC_type1; 1.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR033941; IPMI_cat.
DR NCBIfam; TIGR00170; leuC; 1.
DR PANTHER; PTHR43822:SF9; 3-ISOPROPYLMALATE DEHYDRATASE; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01026};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01026};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01026};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01026};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01026};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_01026};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01026};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01026}; Reference proteome {ECO:0000313|Proteomes:UP000018680}.
FT DOMAIN 8..459
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT BINDING 408
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT BINDING 411
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
SQ SEQUENCE 476 AA; 51869 MW; 376C5F28C829BC6D CRC64;
MAERTLYNKI WENNRVAELP TGQTQLFIGL HMIHEVTSPQ AFDMLRERGL KVAYPQRTFA
TMDHIVPTHS HQRPFADGQA ESMMQAIENN TKDYSIQFFN FQSGKQGVVH VVGPELGLTR
PGMTIACGDS HTSTHGAFGA LAFGIGTSQV RDVLASQCLA MDELKVRRIE IHGKLGTGVT
PKDVALFIIN RLGVKGGIGF VYEYAGEVFD SMSMEGRMTV CNMSIEGGAR AGYVNPDETT
FAYLKGREYA PRGADWDKAV ENWKEYASDQ DAVYDEVVRF HASEIEPMVT WGVTPGQSVG
IHQNLPEPSA MTNDGERRSA ELAYSHMKLS PGQKPSEIAI DVAFIGSCTN GRIEDLRAAA
EVLKGRKVDP AVHAFVVPGS MQVRKQAMDE GLDKIFTAAG FEWREAGCSM CLAMNPDQLK
GDQISASSSN RNFIGRQGSA TGRTLLMSPA MVAAAACNGR VSDIRDFNPM GEALAG
//
