Inosine-5'-monophosphate dehydrogenase - Mycobacterium tuberculosis

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P65167 (IMDH_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. 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:
Inosine-5'-monophosphate dehydrogenase
Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205

Gene names

Name:	guaB
Synonyms:	guaB2
Ordered Locus Names:	Rv3411c, MT3519
ORF Names:	MTCY78.17

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth By similarity. HAMAP-Rule MF_01964
Catalytic activity	Inosine 5'-phosphate + NAD⁺ + H₂O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_01964
Cofactor	Potassium By similarity.
Enzyme regulation	Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH By similarity. Inhibited by the products XMP and NADH. HAMAP-Rule MF_01964
Pathway	Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_01964
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the IMPDH/GMPR family. Contains 2 CBS domains.
Biophysicochemical properties	Kinetic parameters: K_M=128.1 µM for inosine 5'-phosphate Ref.3 K_M=610.5 µM for NAD⁺ pH dependence: Optimum pH is 8-8.5. Temperature dependence: Optimum temperature is 37 degrees Celsius.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Domain	CBS domain Repeat
Ligand	Metal-binding NAD Potassium
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GMP biosynthetic process Inferred from direct assay Ref.3. Source: MTBBASE IMP catabolic process Inferred from direct assay PubMed 20491506 Ref.3. Source: MTBBASE XMP biosynthetic process Inferred from direct assay PubMed 20491506. Source: MTBBASE growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 15525680. Source: MTBBASE
Molecular_function	IMP dehydrogenase activity Inferred from direct assay PubMed 20491506 Ref.3. Source: MTBBASE metal ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 529

529

Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964

PRO_0000093702

Regions

Domain

129 – 185

CBS 1

Domain

189 – 246

CBS 2

Nucleotide binding

334 – 336

NAD By similarity

Region

374 – 376

IMP binding By similarity

Region

397 – 398

IMP binding By similarity

Region

421 – 425

IMP binding By similarity

Sites

Active site

341

Thioimidate intermediate By similarity

Metal binding

336

Potassium; via carbonyl oxygen By similarity

Metal binding

338

Potassium; via carbonyl oxygen By similarity

Metal binding

341

Potassium; via carbonyl oxygen By similarity

Metal binding

511

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Metal binding

512

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Metal binding

513

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Binding site

283

NAD By similarity

Binding site

339

IMP By similarity

Binding site

458

IMP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P65167 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 689A7C7C53993C0A
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FASTA

529

54,867

        10         20         30         40         50         60 
MSRGMSGLED SSDLVVSPYV RMGGLTTDPV PTGGDDPHKV AMLGLTFDDV LLLPAASDVV 

        70         80         90        100        110        120 
PATADTSSQL TKKIRLKVPL VSSAMDTVTE SRMAIAMARA GGMGVLHRNL PVAEQAGQVE 

       130        140        150        160        170        180 
MVKRSEAGMV TDPVTCRPDN TLAQVDALCA RFRISGLPVV DDDGALVGII TNRDMRFEVD 

       190        200        210        220        230        240 
QSKQVAEVMT KAPLITAQEG VSASAALGLL RRNKIEKLPV VDGRGRLTGL ITVKDFVKTE 

       250        260        270        280        290        300 
QHPLATKDSD GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL VVDTAHAHNR LVLDMVGKLK 

       310        320        330        340        350        360 
SEVGDRVEVV GGNVATRSAA AALVDAGADA VKVGVGPGSI CTTRVVAGVG APQITAILEA 

       370        380        390        400        410        420 
VAACRPAGVP VIADGGLQYS GDIAKALAAG ASTAMLGSLL AGTAEAPGEL IFVNGKQYKS 

       430        440        450        460        470        480 
YRGMGSLGAM RGRGGATSYS KDRYFADDAL SEDKLVPEGI EGRVPFRGPL SSVIHQLTGG 

       490        500        510        520 
LRAAMGYTGS PTIEVLQQAQ FVRITPAGLK ESHPHDVAMT VEAPNYYAR

« 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Identification of novel diphenyl urea inhibitors of Mt-GuaB2 active against Mycobacterium tuberculosis." Usha V., Gurcha S.S., Lovering A.L., Lloyd A.J., Papaemmanouil A., Reynolds R.C., Besra G.S. Microbiology 157:290-299(2011) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842583 Genomic DNA. Translation: CAB01012.1. AE000516 Genomic DNA. Translation: AAK47857.1. AL123456 Genomic DNA. Translation: CCP46233.1.
PIR	H70736.
RefSeq	NP_217928.1. NC_000962.3. NP_338043.1. NC_002755.2. YP_006516897.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P65167.
SMR	P65167. Positions 6-526.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv3411c.
Proteomic databases
PRIDE	P65167.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK47857; AAK47857; MT3519.
GeneID	13317015. 887498. 922953.
KEGG	mtc:MT3519. mtu:Rv3411c. mtv:RVBD_3411c.
PATRIC	18129477. VBIMycTub22151_3834.
Organism-specific databases
TubercuList	Rv3411c.
Phylogenomic databases
eggNOG	COG0517.
HOGENOM	HOG000165755.
KO	K00088.
OMA	SAGLKES.
ProtClustDB	PRK05567.
Enzyme and pathway databases
UniPathway	UPA00601; UER00295.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01964. IMPDH.
InterPro	IPR013785. Aldolase_TIM. IPR000644. Cysta_beta_synth_core. IPR005990. IMP_DH. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. [Graphical view]
PANTHER	PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfam	PF00571. CBS. 2 hits. PF00478. IMPDH. 1 hit. [Graphical view]
PIRSF	PIRSF000130. IMPDH. 1 hit.
SMART	SM00116. CBS. 2 hits. [Graphical view]
TIGRFAMs	TIGR01302. IMP_dehydrog. 1 hit.
PROSITE	PS51371. CBS. 2 hits. PS00487. IMP_DH_GMP_RED. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IMDH_MYCTU

Accession

Primary (citable) accession number: P65167
Secondary accession number(s): L0TCG3, Q50715

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 70 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

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

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

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic 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