Dihydroxy-acid dehydratase - Mycobacterium bovis

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P65155 (ILVD_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	Mb0195c

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	575 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 – 575

575

Dihydroxy-acid dehydratase HAMAP MF_00012

PRO_0000103482

Sites

Metal binding

137

Iron-sulfur (4Fe-4S) Potential

Metal binding

214

Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P65155 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 6ECC279BF886A0F1
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FASTA

575

59,352

        10         20         30         40         50         60 
MPQTTDEAAS VSTVADIKPR SRDVTDGLEK AAARGMLRAV GMDDEDFAKP QIGVASSWNE 

        70         80         90        100        110        120 
ITPCNLSLDR LANAVKEGVF SAGGYPLEFG TISVSDGISM GHEGMHFSLV SREVIADSVE 

       130        140        150        160        170        180 
VVMQAERLDG SVLLAGCDKS LPGMLMAAAR LDLAAVFLYA GSILPGRAKL SDGSERDVTI 

       190        200        210        220        230        240 
IDAFEAVGAC SRGLMSRADV DAIERAICPG EGACGGMYTA NTMASAAEAL GMSLPGSAAP 

       250        260        270        280        290        300 
PATDRRRDGF ARRSGQAVVE LLRRGITARD ILTKEAFENA IAVVMAFGGS TNAVLHLLAI 

       310        320        330        340        350        360 
AHEANVALSL QDFSRIGSGV PHLADVKPFG RHVMSDVDHI GGVPVVMKAL LDAGLLHGDC 

       370        380        390        400        410        420 
LTVTGHTMAE NLAAITPPDP DGKVLRALAN PIHPSGGITI LHGSLAPEGA VVKTAGFDSD 

       430        440        450        460        470        480 
VFEGTARVFD GERAALDALE DGTITVGDAV VIRYEGPKGG PGMREMLAIT GAIKGAGLGK 

       490        500        510        520        530        540 
DVLLLTDGRF SGGTTGLCVG HIAPEAVDGG PIALLRNGDR IRLDVAGRVL DVLADPAEFA 

       550        560        570 
SRQQDFSPPP PRYTTGVLSK YVKLVSSAAV GAVCG

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References

[1]

"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.

Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248334 Genomic DNA. Translation: CAD93059.1.
RefSeq	NP_853860.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P65155.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000018096; EBMYCP00000017931; EBMYCG00000018091.
GeneID	1090724.
GenomeReviews	Gene locus Mb0195c in contig BX248333_GR.
KEGG	mbo:Mb0195c.
PATRIC	18002102. VBIMycBov88188_0220.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016366.
HOGENOM	HBG671001.
OMA	NMPGAMI.
ProtClustDB	PRK00911.
Enzyme and pathway databases
BioCyc	MBOV233413:MB0195C-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_MYCBO

Accession

Primary (citable) accession number: P65155
Secondary accession number(s): O07433

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents