Q0S2H7 (Q0S2H7_RHOSR) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Dihydroxy-acid dehydratase 2 HAMAP MF_00012
Short name=DAD 2 HAMAP MF_00012
EC=4.2.1.9 HAMAP MF_00012

Gene names

Name:	ilvD2 HAMAP MF_00012
Ordered Locus Names:	RHA1_ro06484

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP] EMBL ABG98259.1

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	614 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 By similarity. HAMAP MF_00012
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. HAMAP MF_00012

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis HAMAP MF_00012
Ligand	4Fe-4S HAMAP MF_00012 Iron Iron-sulfur Metal-binding
Molecular function	Lyase HAMAP MF_00012 EMBL ABG98259.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: HAMAP valine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW dihydroxy-acid dehydratase activity Inferred from electronic annotation. Source: HAMAP 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	122	1	Iron-sulfur (4Fe-4S) By similarity HAMAP MF_00012
	Metal binding	197	1	Iron-sulfur (4Fe-4S) By similarity HAMAP MF_00012

Sequences

	Sequence		Length	Mass (Da)
	Q0S2H7 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 89E0A7BCC8D3B1BE	FASTA	614	64,750
	10 20 30 40 50 60 MPPLRSRTTT AGRNAAGARA LWRATGMTDS DFGKPIVAIA NSYTQFVPGH VHLKNVGDIV 70 80 90 100 110 120 ADAVRAAGGV PREFHTIAVD DGIAMGHGGM LYSLPSREII ADSVEYMVNA HTADALVCIS 130 140 150 160 170 180 NCDKITPGML NAALRLNVPT VFVSGGPMEA GKAVVVNGVA QAPTDLITAI SASANDEVDE 190 200 210 220 230 240 EGLSEVERSA CPTCGSCSGM FTANSMNCLT EALGLALPGN GSTLATHEAR RALFTRAGTT 250 260 270 280 290 300 VVEAALRYYR DEDDSVLPRN IATPAAFRNA MALDVAMGGS TNTVLHTLAA AQEGEVYDFD 310 320 330 340 350 360 LDKIDEISRK VPCLSKVSPN SDYHMEDVHR AGGIPAILGE LRRAGLLESD VSTVHTESFD 370 380 390 400 410 420 EWLDTWDIRS GKASDEAVEL FHAAPGGVRT TEPFSTNNRW SSLDTDAANG CIRDFEHKHT 430 440 450 460 470 480 VEGGLAVLRG NIAVDGAVIK TAGIDEDLFH FQGPARVVES QEEAVSVILG KKIQPGEVLV 490 500 510 520 530 540 VRYEGPAGGP GMQEMLHPTA FLKGSGLGKK CALITDGRFS GGSSGLSIGH ISPEAASGGA 550 560 570 580 590 600 IGLVEDGDQI LIDIATRTLK LLVDDAVLAE RRAKMESSER PWQPVNRERT VTTALRAYAA 610 LATSADKGAV RQVP

References

[1]

"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed: 17030794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000431 Genomic DNA. Translation: ABG98259.1.
RefSeq	YP_706417.1. NC_008268.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0S2H7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4224035.
GenomeReviews	Gene locus RHA1_ro06484 in contig CP000431_GR.
KEGG	rha:RHA1_ro06484.
PATRIC	23211929. VBIRhoJos26306_6538.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0129.
HOGENOM	HBG671001.
OMA	SQDCRWP.
PhylomeDB	Q0S2H7.
ProtClustDB	PRK12448.
Enzyme and pathway databases
BioCyc	RSP101510:RHA1_RO06484-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

Q0S2H7_RHOSR

Accession

Primary (citable) accession number: Q0S2H7

Entry history

Integrated into UniProtKB/TrEMBL:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	December 14, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)