ID A9AZ33_HERA2 Unreviewed; 471 AA.
AC A9AZ33;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 104.
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 OrderedLocusNames=Haur_4441 {ECO:0000313|EMBL:ABX07073.1};
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC Herpetosiphonaceae; Herpetosiphon.
OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX07073.1, ECO:0000313|Proteomes:UP000000787};
RN [1] {ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABX07073.1, ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RX PubMed=22675585; DOI=10.4056/sigs.2194987;
RA Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT "Complete genome sequence of the filamentous gliding predatory bacterium
RT Herpetosiphon aurantiacus type strain (114-95(T)).";
RL Stand. Genomic Sci. 5:356-370(2011).
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; CP000875; ABX07073.1; -; Genomic_DNA.
DR AlphaFoldDB; A9AZ33; -.
DR STRING; 316274.Haur_4441; -.
DR KEGG; hau:Haur_4441; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_0; -.
DR InParanoid; A9AZ33; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000000787; 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}.
FT DOMAIN 7..462
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 352
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT BINDING 412
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT BINDING 415
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
SQ SEQUENCE 471 AA; 50304 MW; 57D38C10FDCEEEDD CRC64;
MAKTLFEKIW DAHVVQAADA ESPATLYIDL HLVHEVTSPQ AFTMLRERGL TVRRPAQTLA
TMDHSTPTTP RGADGIIPVT DAIARKQLDQ LIKNCSDFGI PLYNLGTENQ GIVHVIGPEQ
GYTQPGMTIV CGDSHTSTHG AFGALAFGIG TSEVGHVLAT QCLLQQKPQT AEIRIDGTLR
PGVTAKDIIL AIIAKIGVGG GTGYVLEYTG SAIRALTMEE RMTICNMSIE GGARAGLIAP
DETTFAWLKD RPHTPKGEAW DAAVEYWRTL PSDEGATYDL QVVLNADELA PMITYGTNPG
MGIPVTGNVP APSDLADDSQ RMALDKALNY MGLQPNQSLI GQKVDVVFLG SCTNSRISDL
RAAAKVIEGK KVADGLRMLV VPGSQQVKRQ AEAEGLDQIF RAAGAEWREA GCSMCIAMNG
DQLQPGQYAV STSNRNFEGR QGKGGRTFLA SPLTAAATAI NGHIVDVREI L
//
