Q04RA5 (ILVD_LEPBJ) 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:	LBJ_2063

Organism

Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]

Taxonomic identifier

355277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Leptospiraceae › Leptospira › Leptospira borgpetersenii › Leptospira borgpetersenii serovar Hardjo-bovis

Protein attributes

Sequence length	560 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-Rule 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-Rule MF_00012 Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4. HAMAP-Rule 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	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
Molecule processing
	Chain	1 – 560	560	Dihydroxy-acid dehydratase HAMAP-Rule MF_00012		PRO_1000000998
Sites
	Metal binding	125	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	197	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q04RA5 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: A00F61DB3743235D	FASTA	560	59,445
	10 20 30 40 50 60 MSDILKKRSS MTTDGDNRAP NRAMLRAVGF TDEDFHKPMI GIASTWSEVT PCNIHINKLA 70 80 90 100 110 120 EKVKEGVRTA GGVPQIYGTI TVSDGITMGH EGMHFSLPSR EVIADSIEIV SNAMRHDGVI 130 140 150 160 170 180 AIGGCDKNMP GCLMALCRID APSIFVYGGT ILPGHCDGQD VDIVSIFEAV GKFNAGKISR 190 200 210 220 230 240 EEFIRIEQNA CPGAGSCGGM YTANTMSSAI EALGMSLPGS ASMPAVSSRK SEDCYEAGKA 250 260 270 280 290 300 LINLIQKGVT PKRILTKKAF ENAITVVLVL GGSTNAVLHL IAIAKEIGVD LTLEDFDRIS 310 320 330 340 350 360 KKTPHLADLK PGGRYAMTDL DKVGGVHGVM KYLLKEGMLH GDCLTVTGKT IAENLMDMPD 370 380 390 400 410 420 LVPNQTIVRK KSEALHPSGP LVILKGNLAP EGAVAKISGL KKISITGPAK VFESEDDCFN 430 440 450 460 470 480 AIMTDQIKPG DVIIIRYEGP KGGPGMREML AVTSALVGKG LGEDVGLMTD GRFSGGTHGL 490 500 510 520 530 540 VVGHISPEAF DGGPIAIVQN GDAVTIDSGK NLLQVEISQE EIQKRLKNWK PIEPRYKSGV 550 560 LAKYAKLVQS ATNGAITNLL

References

[1]

"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential." Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B. Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JB197.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000350 Genomic DNA. Translation: ABJ76565.1.
RefSeq	YP_801323.1. NC_008510.1.
3D structure databases
ProteinModelPortal	Q04RA5.
ModBase	Search...
Protein-protein interaction databases
STRING	355277.LBJ_2063.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABJ76565; ABJ76565; LBJ_2063.
GeneID	4410841.
KEGG	lbj:LBJ_2063.
PATRIC	22359860. VBILepBor13265_2634.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0129.
HOGENOM	HOG000173155.
KO	K01687.
OMA	NMPGAMI.
ProtClustDB	PRK00911.
Enzyme and pathway databases
BioCyc	LBOR355277:GHYM-2317-MONOMER.
UniPathway	UPA00047; UER00057. UPA00049; UER00061.
Family and domain databases
HAMAP	MF_00012. IlvD.
InterPro	IPR015928. Aconitase/3IPM_dehydase_swvl. IPR004404. DihydroxyA_deHydtase. IPR000581. DiOHA_6PGluconate_deHydtase. IPR020558. DiOHA_6PGluconate_deHydtase_CS. [Graphical view]
PANTHER	PTHR21000. PTHR21000. 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_LEPBJ

Accession

Primary (citable) accession number: Q04RA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program