LEUD_MYCTU
ID LEUD_MYCTU Reviewed; 198 AA.
AC P9WK95; L0TE54; O53236; P65277;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=3-isopropylmalate dehydratase small subunit;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE Short=IPMI;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leuD; OrderedLocusNames=Rv2987c; ORFNames=MTV012.01c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PUPYLATION AT LYS-154, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45792.1; -; Genomic_DNA.
DR PIR; F70853; F70853.
DR RefSeq; NP_217503.1; NC_000962.3.
DR RefSeq; WP_003415110.1; NZ_NVQJ01000041.1.
DR PDB; 3H5E; X-ray; 2.00 A; A/B=2-156.
DR PDB; 3H5H; X-ray; 2.50 A; A/B=2-186.
DR PDB; 3H5J; X-ray; 1.20 A; A/B=2-168.
DR PDBsum; 3H5E; -.
DR PDBsum; 3H5H; -.
DR PDBsum; 3H5J; -.
DR AlphaFoldDB; P9WK95; -.
DR SMR; P9WK95; -.
DR STRING; 83332.Rv2987c; -.
DR PaxDb; P9WK95; -.
DR DNASU; 888225; -.
DR GeneID; 45426976; -.
DR GeneID; 888225; -.
DR KEGG; mtu:Rv2987c; -.
DR TubercuList; Rv2987c; -.
DR eggNOG; COG0066; Bacteria.
DR OMA; AFTTHTG; -.
DR PhylomeDB; P9WK95; -.
DR BRENDA; 4.2.1.33; 3445.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IMP:MTBBASE.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR HAMAP; MF_01031; LeuD_type1; 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 Pfam; PF00694; Aconitase_C; 1.
DR TIGRFAMs; TIGR00171; leuD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Isopeptide bond;
KW Leucine biosynthesis; Lyase; Reference proteome; Ubl conjugation.
FT CHAIN 1..198
FT /note="3-isopropylmalate dehydratase small subunit"
FT /id="PRO_0000141840"
FT CROSSLNK 154
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3H5J"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3H5J"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3H5J"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3H5J"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3H5E"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:3H5J"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:3H5J"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:3H5J"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3H5J"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:3H5J"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3H5J"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3H5J"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:3H5J"
SQ SEQUENCE 198 AA; 21780 MW; 705B4A11FB41DB8B CRC64;
MEAFHTHSGI GVPLRRSNVD TDQIIPAVFL KRVTRTGFED GLFAGWRSDP AFVLNLSPFD
RGSVLVAGPD FGTGSSREHA VWALMDYGFR VVISSRFGDI FRGNAGKAGL LAAEVAQDDV
ELLWKLIEQS PGLEITANLQ DRIITAATVV LPFKIDDHSA WRLLEGLDDI ALTLRKLDEI
EAFEGACAYW KPRTLPAP
