Q82E99 (ILVD_STRAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroxy-acid dehydratase
Short name=DAD
EC=4.2.1.9

Gene names

Name:	ilvD
Ordered Locus Names:	SAV_4716

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	617 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O. HAMAP MF_00012
Cofactor	Binds 1 4Fe-4S cluster Potential.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4. HAMAP MF_00012 Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4. HAMAP MF_00012
Sequence similarities	Belongs to the IlvD/Edd family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW dihydroxy-acid dehydratase activity Inferred from electronic annotation. Source: EC 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 – 617	617	Dihydroxy-acid dehydratase HAMAP MF_00012		PRO_0000103513
Sites
	Metal binding	123	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	197	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q82E99 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 60B293C8034FBABA	FASTA	617	65,370
	10 20 30 40 50 60 MPELRSRTVT HGRNMAGARA LMRASGVPGA DIGRKPIIAV ANSFTEFVPG HTHLQPVGRI 70 80 90 100 110 120 VSEAITAAGG IAREFNTIAV DDGIAMGHGG MLYSLPSRDL IADSVEYMVE AHCADALICI 130 140 150 160 170 180 SNCDKITPGM LMAALRLNIP TVFVSGGPME SGRATLVDGT VRTLDLVDAI SDAVNDKISD 190 200 210 220 230 240 EDILRIEENA CPTCGSCSGM FTANSMNCLT EAIGLSLPGN GSVLATHTAR KGLYEDAART 250 260 270 280 290 300 VVDITRRYYE QDDESVLPRN IATHAAFENA MALDIAMGGS TNTILHLLAA AQEAGVPFGL 310 320 330 340 350 360 DEINEVSRRV PCLAKVAPNV AKDRTYYMED VHRAGGIPAL LGELHRAGLL NEDVHSVHSP 370 380 390 400 410 420 SLSDWLKTWD VRAGSPSPEA IELWHAAPGC VRSSEAFSQS ERWEALDEDA EGGCIRSAEH 430 440 450 460 470 480 AYSKDGGLAV LKGNLAVDGC VVKTAGVDES IWTFEGPAVV CESQDEAVDK ILRKEITHGD 490 500 510 520 530 540 VVVIRYEGPK GGPGMQEMLY PTSFLKGRGL GKTCALITDG RFSGGTSGLS IGHASPEAAS 550 560 570 580 590 600 GGTIALVQDG DRIRIDIPNR TIDLLVDEAE LSRRDQALNG VYAPVNRERK VSAALRAYAA 610 MATSADKGAV RDVSKLG

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC72428.1.
RefSeq	NP_825893.1. NC_003155.4.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1211052.
GenomeReviews	Gene locus SAV_4716 in contig BA000030_GR.
KEGG	sma:SAV_4716.
NMPDR	fig|227882.1.peg.4719.
PATRIC	23723307. VBIStrAve112782_5032.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG671001.
OMA	SQDCRWP.
ProtClustDB	PRK12448.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV4716-MONOMER.
Family and domain databases
HAMAP	MF_00012. IlvD. [Tree]
InterPro	IPR015928. Aconitase/3IPM_dehydase_swvl. IPR004404. DihydroxyA_deHydtase. IPR000581. DiOHA_6PGluconate_deHydtase. IPR020558. DiOHA_6PGluconate_deHydtase_CS. [Graphical view]
KO	K01687.
PANTHER	PTHR21000. ILVD_EDD_family. 1 hit.
Pfam	PF00920. ILVD_EDD. 1 hit. [Graphical view]
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
TIGRFAMs	TIGR00110. IlvD. 1 hit.
PROSITE	PS00886. ILVD_EDD_1. 1 hit. PS00887. ILVD_EDD_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILVD_STRAW

Accession

Primary (citable) accession number: Q82E99

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program