Q63DX8 (LEU1_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-isopropylmalate synthase
EC=2.3.3.13

Alternative name(s):
Alpha-IPM synthase
Alpha-isopropylmalate synthase

Gene names

Name:	leuA
Ordered Locus Names:	BCE33L1285

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus cereus

Protein attributes

Sequence length	506 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) By similarity. HAMAP-Rule MF_01025
Catalytic activity	Acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA. HAMAP-Rule MF_01025
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. HAMAP-Rule MF_01025
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	2-isopropylmalate synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 506	506	2-isopropylmalate synthase HAMAP-Rule MF_01025		PRO_1000149134

Sequences

	Sequence		Length	Mass (Da)
	Q63DX8 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 4AB125DDC8596189	FASTA	506	55,401
	10 20 30 40 50 60 MKKILFMDTT LRDGEQSPGV NLNEQEKLQI ARQLERLGIH VMEAGFAAAS EGDFQSVKRI 70 80 90 100 110 120 ANTIQNATVM SLARAKESDI RRAYEAVKGA VSPRLHVFLA TSDIHMKYKL CMSKEDVLDS 130 140 150 160 170 180 IYRSVTLGKS LFPTVQFSAE DATRTARDFL AEAVEVAIRA GANVINIPDT VGYTNPEEYY 190 200 210 220 230 240 SLFKYLQESV PSYEKAIFSC HCHDDLGMAV ANSLAAVEGG ALQVEGTING IGERAGNAAL 250 260 270 280 290 300 EEVAVALHIR KDFYKAEPSM TLKEIKATST LVSRLTGMVV PKNKAIVGAN AFAHESGIHQ 310 320 330 340 350 360 DGVLKEVTTY EIIEPALVGE SQNLFVLGKH SGRHAFTEKM KELGYEFTND ERDAVFEAFK 370 380 390 400 410 420 KLADRKKEIT EEDLRALMLG EAAFAAQQYN ITQLQVHFVS NSTQCATVVL KDEEGNVFED 430 440 450 460 470 480 AATGSGSIEA IYNAIQRILG LECELADYRI QSITQGQDAL AHVHVELKEG AHQVSGFGVA 490 500 QDVLEASARA YVHAAGKLKS FIQLVK

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZK / E33L.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU18963.1.
RefSeq	YP_082884.1. NC_006274.1.
3D structure databases
ProteinModelPortal	Q63DX8.
ModBase	Search...
Protein-protein interaction databases
STRING	288681.BCZK1285.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU18963; AAU18963; BCE33L1285.
GeneID	3023896.
KEGG	bcz:BCZK1285.
PATRIC	18886034. VBIBacCer95304_1356.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0119.
KO	K01649.
OMA	TKEYPAT.
ProtClustDB	PRK00915.
Enzyme and pathway databases
BioCyc	BCER288681:GHG7-1793-MONOMER.
UniPathway	UPA00048; UER00070.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01025. LeuA_type1.
InterPro	IPR013709. 2-isopropylmalate_synth_dimer. IPR002034. AIPM/Hcit_synth_CS. IPR013785. Aldolase_TIM. IPR005671. LeuA_bact_synth. IPR000891. PYR_CT. [Graphical view]
Pfam	PF00682. HMGL-like. 1 hit. PF08502. LeuA_dimer. 1 hit. [Graphical view]
SMART	SM00917. LeuA_dimer. 1 hit. [Graphical view]
SUPFAM	SSF110921. 2-isopropylmalate_synth_dimer. 1 hit.
TIGRFAMs	TIGR00973. leuA_bact. 1 hit.
PROSITE	PS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit. PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit. PS50991. PYR_CT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEU1_BACCZ

Accession

Primary (citable) accession number: Q63DX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	October 25, 2004
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program