Q74BX5 (LEUC_GEOSL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-isopropylmalate dehydratase large subunit
EC=4.2.1.33

Alternative name(s):
Alpha-IPM isomerase
Short name=IPMI
Isopropylmalate isomerase

Gene names

Name:	leuC
Ordered Locus Names:	GSU1903

Organism

Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) [Reference proteome] [HAMAP]

Taxonomic identifier

243231 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter › Geobacter sulfurreducens

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. HAMAP-Rule MF_01027
Catalytic activity	(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01027
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01027
Subunit structure	Heterodimer of LeuC and LeuD By similarity.
Sequence similarities	Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: HAMAP 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 427	427	3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01027		PRO_1000063649
Sites
	Metal binding	308	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	368	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	371	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q74BX5 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: D6F9FD70E5B93B54	FASTA	427	46,173
	10 20 30 40 50 60 MGKTIAEKIF ASHLVDEPFA GTKVLRLDVV MCHEITTPIA IADLMARGKD RVFDPTKIKA 70 80 90 100 110 120 VIDHVTPSKD SKTATQAKML RDWARRHGIV DFFDVGANGV CHALFPEKGF IRPGYTVIMG 130 140 150 160 170 180 DSHTCTHGAF GAFAAGIGTT DLEVGILKGV CAFREPKTIR INLNGSLPEG VYAKDVILHV 190 200 210 220 230 240 IGRIGVNGAT DRVMEFRGSV VDTMTMESRM TLCNMAIEAG GTSGICMPDM VTVDYLWPFL 250 260 270 280 290 300 KDEYQSREAA LAAFSLWRSD EDAVYEQVLD FDVSSLEPIV TFGYKPDQVK PVSEIAGTPV 310 320 330 340 350 360 DQVYLGSCTN GRLEDLRIAA RILKGKKIAP TVRGILSPAT PKIYQDAMRE GLIDIFMEAG 370 380 390 400 410 420 FCVTNPTCGA CLGMSNGVLA EGEVCASTTN RNFMGRMGKG GMVHLMSPAT SAATAIEGKI ADPRKYL

References

[1]

"Genome of Geobacter sulfurreducens: metal reduction in subsurface environments." Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.L., Kolonay J.F. , Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R., Fraser C.M. Science 302:1967-1969(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51573 / DSM 12127 / PCA.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017180 Genomic DNA. Translation: AAR35279.1.
RefSeq	NP_952952.1. NC_002939.5.
3D structure databases
ProteinModelPortal	Q74BX5.
ModBase	Search...
Protein-protein interaction databases
STRING	243231.GSU1903.
Protocols and materials databases
DNASU	2688457.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAR35279; AAR35279; GSU1903.
GeneID	2688457.
KEGG	gsu:GSU1903.
PATRIC	22026671. VBIGeoSul17553_1941.
Phylogenomic databases
eggNOG	COG0065.
HOGENOM	HOG000226971.
KO	K01703.
OMA	ANGVCHA.
ProtClustDB	PRK00402.
Enzyme and pathway databases
BioCyc	GSUL243231:GH27-1939-MONOMER.
UniPathway	UPA00048; UER00071.
Family and domain databases
Gene3D	3.30.499.10. 2 hits. 3.40.1060.10. 1 hit.
HAMAP	MF_01027. LeuC_type2.
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR011826. HAcnase/IPMdehydase_lsu_prok. IPR006251. Homoacnase/IPMdehydase_lsu. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF6. PTHR11670:SF6. 1 hit.
Pfam	PF00330. Aconitase. 2 hits. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR01343. hacA_fam. 1 hit. TIGR02086. IPMI_arch. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEUC_GEOSL

Accession

Primary (citable) accession number: Q74BX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program