ID A0A2I9DWH9_9FLAO Unreviewed; 469 AA.
AC A0A2I9DWH9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ECO:0000313|EMBL:GBF19724.1};
GN ORFNames=C21_01894 {ECO:0000313|EMBL:GBF19724.1};
OS Arenibacter sp. NBRC 103722.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=1113929 {ECO:0000313|EMBL:GBF19724.1, ECO:0000313|Proteomes:UP000095208};
RN [1] {ECO:0000313|EMBL:GBF19724.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF19724.1};
RA Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H., Amachi S.;
RT "Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-
RT Accumulating Bacterium Isolated from Surface Marine Sediment.";
RL Genome Announc. 4:e01155-16(2016).
RN [2] {ECO:0000313|EMBL:GBF19724.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF19724.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF19724.1}.
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DR EMBL; BDGL02000007; GBF19724.1; -; Genomic_DNA.
DR RefSeq; WP_031444078.1; NZ_BDGL02000007.1.
DR AlphaFoldDB; A0A2I9DWH9; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000095208; Unassembled WGS sequence.
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; 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:UP000095208}.
FT DOMAIN 7..455
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 345
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT BINDING 405
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"
SQ SEQUENCE 469 AA; 50835 MW; F334474DE05C38EC CRC64;
MKKTLFDKVW DSHVVHKIEN GPDVLFIDRH MVHEVTSPVA FLGIKSRGIP VMYPGRTFAT
ADHNTPTINQ HLPVKDPLSA NQLKALEENS KAHGISYWGL GHEKNGIVHV VGPEYGITQP
GATIVCGDSH TSTHGAFGAI AFGIGTSEVE MVLATQCIMQ QKAKSMRINV NGKLSKGVTP
KDVALYIISK LTTSGATGYF VEYAGDVFRN MTMEGRMTVC NLSIEMGARG GMIAPDEKTF
EYIKGREFTP VGADWDKAME YWKTLKTDED ATFDKEITFD AADIEPMITY GTNPGMGIGI
SNGIPQAESV EGGVATYKKS LQYMAFNEGD NMIGKPIDFV FLGSCTNGRI EDFRAFASIV
KGRKKADNVT AWLVPGSHKV ESAIKEEGIL DILHEAGFEL REPGCSACLA MNDDKVPAGK
YAVSTSNRNF EGRQGPGSRT LLASPLVAAA AAVTGKVTDP RELMQEELV
//
