NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity).
CATALYTIC ACTIVITY: 3-carboxy-2-hydroxy-4-methylpentanoate + NAD⁺ = 3-carboxy-4-methyl-2-oxopentanoate + NADH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000117; ABA22597.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_323492.1; -.

3D structure databases

ModBase

Q3M8T9.

Enzyme and pathway databases

BioCyc

AVAR240292:AVA_2987-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003862;	Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0009098;	Biological process: leucine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01033; -; 1.
PBIL [Tree]

InterPro

IPR004429; 3-isopropylmalate_DHase.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF13; IPMDH; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00169; leuB; 1.

PROSITE

PS00470; IDH_IMDH; 1.

BLOCKS

Q3M8T9.

Genome annotation databases

GeneID

3681222; -.

GenomeReviews

CP000117_GR; Ava_2987.

KEGG

ava:Ava_2987; -.

NMPDR

fig|240292.3.peg.2045; -.

Phylogenomic databases

HOGENOM

Q3M8T9; -.

Genome annotation databases

CMR

Q3M8T9; Ava_2987.

Other

ProtoNet

Q3M8T9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 362`	`362`	`3-isopropylmalate dehydrogenase.`	`PRO_0000250100`
`NP_BIND`	`78 91`	`14`	`NAD (By similarity).`
`NP_BIND`	`284 296`	`13`	`NAD (By similarity).`
`METAL`	`226 226`		`Magnesium or manganese (By similarity).`
`METAL`	`250 250`		`Magnesium or manganese (By similarity).`
`METAL`	`254 254`		`Magnesium or manganese (By similarity).`
`BINDING`	`98 98`		`Substrate (By similarity).`
`BINDING`	`108 108`		`Substrate (By similarity).`
`BINDING`	`136 136`		`Substrate (By similarity).`
`BINDING`	`226 226`		`Substrate (By similarity).`
`SITE`	`143 143`	`1`	`Important for catalysis (By similarity).`
`SITE`	`194 194`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 362 AA [This is the length of the unprocessed precursor]

Molecular weight: 38849 Da [This is the MW of the unprocessed precursor]

CRC64: F95CB20C7827D793 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQNYRITLL PGDGIGPEIM AVAVDVLKVV GQQFDIQFDF QEALIGGAAI DATGEPLPSA 

        70         80         90        100        110        120 
TLDTCRQSDA VLLAAIGGYK WDSLPPHQRP EGGLLGLRAG LELFANLRPA QILPQLIDAS 

       130        140        150        160        170        180 
TLKREVVEGV DIMVVRELTG GIYFGKPRGI FTTETGEKRG VNTMVYTESE IDRIGRIAFE 

       190        200        210        220        230        240 
TARKRRGKLC SVDKANVLDV SQLWRDRITK LSQEYPDVEL SHLYVDNAAM QLVRAPKQFD 

       250        260        270        280        290        300 
TIVTGNLFGD ILSDAAAMLT GSIGMLPSAS LGASGPGVFE PVHGSAPDIA GLDKANPLAQ 

       310        320        330        340        350        360 
VLSAAMMLRY ALNQPQAADK IEQAVLQVLE QGDRTGDIMS VGMNLLGCRA MGDSLIKALE 


KS

Q3M8T9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools