D9QTJ6 (D9QTJ6_ACEAZ) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01027
EC=4.2.1.33 HAMAP-Rule MF_01027

Alternative name(s):
Alpha-IPM isomerase HAMAP-Rule MF_01027
Isopropylmalate isomerase HAMAP-Rule MF_01027

Gene names

Name:	leuC HAMAP-Rule MF_01027
Ordered Locus Names:	Acear_0209

Organism

Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288) [Complete proteome] [HAMAP] EMBL ADL11760.1

Taxonomic identifier

574087 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Halanaerobiales › Halobacteroidaceae › Acetohalobium › Acetohalobium arabaticum

Protein attributes

Sequence length	420 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. HAMAP-Rule MF_01027 SAAS SAAS001030
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. HAMAP-Rule MF_01027
Sequence similarities	Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily. HAMAP-Rule MF_01027

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis HAMAP-Rule MF_01027
Ligand	4Fe-4S HAMAP-Rule MF_01027 SAAS SAAS001030 Iron Iron-sulfur Metal-binding
Molecular function	Lyase HAMAP-Rule MF_01027 SAAS SAAS001030 EMBL ADL11760.1
Technical term	Complete 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
Sites
	Metal binding	300	1	Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01027
	Metal binding	360	1	Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01027
	Metal binding	363	1	Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01027

Sequences

	Sequence		Length	Mass (Da)
	D9QTJ6 [UniParc]. Last modified October 5, 2010. Version 1. Checksum: 67586F170AB1AB75	FASTA	420	45,422
	10 20 30 40 50 60 MGMTMVEKIL ADHAGREEVQ PGELINARLD IVLGNDVTTP VAIKEFDKIG VDEVFDKERV 70 80 90 100 110 120 VIVPDHFAPN KDINSAEQCK FIRGFAEEKE LVNYFEIGEM GIEHCLLPEQ GLVLPGDAVI 130 140 150 160 170 180 GADSHTCTYG ALGAFATGVG STDMAAGMAT GEAWFKVPET IKFVYNGELN DWVGGKDLIL 190 200 210 220 230 240 YTIGDIGVDG ALYKAMEFTG EVIENLPMDH RFTMSNMAIE AGGKCGLIEP DQTTIDYVED 250 260 270 280 290 300 RAQRDYKLYQ SDEDAEYDEI IEYDVSQIEP QVAFPHLPEN TRGISEVGEV EIDQAVIGSC 310 320 330 340 350 360 TNGRLGDLRL AAKVLEGKKA ADNVRLIVFP GTQEIYKQAM KEGLIETLID AGAAVSTPTC 370 380 390 400 410 420 GPCLGGHMGI LAEGERAIAT TNRNFVGRMG HPESEVYLSN PAVAAASAIK GKIVSPKEVI

References

[1]

"Complete genome sequence of Acetohalobium arabaticum type strain (Z-7288)." Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A., Glavina Del Rio T., Nolan M., Tice H., Cheng J., Han C., Brambilla E., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Bruce D. , Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Rohde M., Goker M., Spring S., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H. Stand. Genomic Sci. 3:57-65(2010) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49924 / DSM 5501 / Z-7288.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002105 Genomic DNA. Translation: ADL11760.1.
RefSeq	YP_003826825.1. NC_014378.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADL11760; ADL11760; Acear_0209.
GeneID	9512211.
KEGG	aar:Acear_0209.
PATRIC	42134535. VBIAceAra30843_0225.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000226971.
KO	K01703.
Enzyme and pathway databases
BioCyc	AARA574087:GHPK-235-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. IPR011823. IsopropMal_deHydtase_lsu_bac. [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. TIGR02083. LEU2. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

D9QTJ6_ACEAZ

Accession

Primary (citable) accession number: D9QTJ6

Entry history

Integrated into UniProtKB/TrEMBL:	October 5, 2010
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)