Isochorismate synthase/isochorismate-pyruvate lyase mbtI

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Q7D785 (MBTI_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. History...

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

Documents (3) |

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:
Isochorismate synthase/isochorismate-pyruvate lyase mbtI
EC=4.1.3.-
EC=5.4.4.2

Alternative name(s):
Mycobactin synthase protein I
Salicylate synthase mbtI

Gene names

Name:	mbtI
Synonyms:	trpE2
Ordered Locus Names:	Rv2386c, MT2454

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates the production of salicylate from chorismate via an isochorismate intermediate. Presents both isochorismate synthase and isochorismate-pyruvate lyase activities. Salycilate is the starter unit in the production of the virulence-conferring salicylate-based siderophore mycobactin. Ref.5
Catalytic activity	Chorismate = isochorismate. Ref.5 Isochorismate = salicylate + pyruvate. Ref.5
Cofactor	Magnesium. Ref.5
Pathway	Siderophore biosynthesis; mycobactin biosynthesis.
Subunit structure	Monomer. Ref.5
Induction	Induced by iron starvation conditions and during infection of human THP-1 macrophages. Transcriptionally repressed by ideR and iron. Ref.3
Disruption phenotype	Cells lacking this gene display a reduction in salicylic acid biosynthesis and a drastic decrease in production of mycobactin compared with the wild-type strain. Ref.4
Sequence similarities	Belongs to the anthranilate synthase component I family. Salicylate synthase subfamily.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase Lyase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	cellular response to iron ion starvation Inferred from expression pattern Ref.3. Source: MTBBASE growth Inferred from mutant phenotype. Source: MTBBASE response to host immune response Inferred from expression pattern Ref.3. Source: MTBBASE salicylic acid biosynthetic process Inferred from direct assay Ref.5. Source: MTBBASE siderophore biosynthetic process from catechol Inferred from direct assay Ref.5. Source: MTBBASE
Cellular component	plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	chorismate mutase activity Inferred from direct assay. Source: MTBBASE isochorismate pyruvate lyase activity Inferred from direct assay Ref.5. Source: MTBBASE isochorismate synthase activity Inferred from direct assay Ref.5. Source: MTBBASE magnesium ion binding Inferred from direct assay Ref.5. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Isochorismate synthase/isochorismate-pyruvate lyase mbtI

PRO_0000262086

Sites

Metal binding

294

Magnesium Probable

Metal binding

297

Magnesium Probable

Metal binding

431

Magnesium Probable

Metal binding

434

Magnesium Probable

Binding site

271

Salicylate Probable

Binding site

334

Salicylate Probable

Binding site

385

Pyruvate

Binding site

405

Pyruvate

Binding site

438

Pyruvate

Secondary structure

450

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q7D785 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 79D95307E025D28A
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FASTA

450

48,754

        10         20         30         40         50         60 
MSELSVATGA VSTASSSIPM PAGVNPADLA AELAAVVTES VDEDYLLYEC DGQWVLAAGV 

        70         80         90        100        110        120 
QAMVELDSDE LRVIRDGVTR RQQWSGRPGA ALGEAVDRLL LETDQAFGWV AFEFGVHRYG 

       130        140        150        160        170        180 
LQQRLAPHTP LARVFSPRTR IMVSEKEIRL FDAGIRHREA IDRLLATGVR EVPQSRSVDV 

       190        200        210        220        230        240 
SDDPSGFRRR VAVAVDEIAA GRYHKVILSR CVEVPFAIDF PLTYRLGRRH NTPVRSFLLQ 

       250        260        270        280        290        300 
LGGIRALGYS PELVTAVRAD GVVITEPLAG TRALGRGPAI DRLARDDLES NSKEIVEHAI 

       310        320        330        340        350        360 
SVRSSLEEIT DIAEPGSAAV IDFMTVRERG SVQHLGSTIR ARLDPSSDRM AALEALFPAV 

       370        380        390        400        410        420 
TASGIPKAAG VEAIFRLDEC PRGLYSGAVV MLSADGGLDA ALTLRAAYQV GGRTWLRAGA 

       430        440        450 
GIIEESEPER EFEETCEKLS TLTPYLVARQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages." Gold B., Rodriguez G.M., Marras S.A.E., Pentecost M., Smith I. Mol. Microbiol. 42:851-865(2001) [PubMed: 11722747] [Abstract] Cited for: INDUCTION. Strain: ATCC 25618 / H37Rv.
[4]	"Roles of trpE2, entC and entD in salicylic acid biosynthesis in Mycobacterium smegmatis." Nagachar N., Ratledge C. FEMS Microbiol. Lett. 308:159-165(2010) [PubMed: 20487026] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[5]	"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase." Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S. J. Bacteriol. 188:6081-6091(2006) [PubMed: 16923875] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH PYRUVATE, FUNCTION, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY. Strain: ATCC 25618 / H37Rv.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000516 Genomic DNA. Translation: AAK46749.1.
BX842579 Genomic DNA. Translation: CAE55483.1.

RefSeq

NP_336935.1. NC_002755.2.
YP_177877.1. NC_000962.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G5F	X-ray	1.80	A/B/C/D	2-450	[»]
2I6Y	X-ray	2.50	A	2-450	[»]
3LOG	X-ray	1.73	A/B/C/D	1-449	[»]

ProteinModelPortal

Q7D785.

SMR

Q7D785. Positions 15-449.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000000542; EBMYCP00000000542; EBMYCG00000000542.
EBMYCT00000069235; EBMYCP00000067294; EBMYCG00000069230.

GeneID

885823.
925895.

GenomeReviews

Gene locus MT2454 in contig AE000516_GR.
Gene locus Rv2386c in contig AL123456_GR.

KEGG

mtc:MT2454.
mtu:Rv2386c.

PATRIC

18127148. VBIMycTub22151_2682.

TIGR

MT2454.

Organism-specific databases

TubercuList

Rv2386c.

Phylogenomic databases

GeneTree

EBGT00050000015088.

HOGENOM

HBG326929.

OMA

TPEREFE.

PhylomeDB

Q7D785.

ProtClustDB

PRK07912.

Family and domain databases

InterPro

IPR005801. ADC_synthase.
IPR019999. Anth_synth_I.
IPR015890. Chorismate-bd_C.
IPR019996. Salicylate_synthase.
[Graphical view]

Gene3D

G3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.

K04781.

PANTHER

PTHR11236:SF5. PTHR11236:SF5. 1 hit.

Pfam

PF00425. Chorismate_bind. 1 hit.
[Graphical view]

PRINTS

PR00095. ANTSNTHASEI.

SUPFAM

SSF56322. TRPE_1_chor_bd. 1 hit.

TIGRFAMs

TIGR03494. Salicyl_syn. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MBTI_MYCTU

Accession

Primary (citable) accession number: Q7D785
Secondary accession number(s): Q79FE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 65 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents