Inosine-5'-monophosphate dehydrogenase - Staphylococcus aureus (strain N315)

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P99106 (IMDH_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. 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:
Inosine-5'-monophosphate dehydrogenase
Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205

Gene names

Name:	guaB
Ordered Locus Names:	SA0375

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length	488 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. 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.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Domain	CBS domain Repeat
Ligand	Metal-binding NAD Potassium
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	GMP biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	IMP dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 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 – 488

488

Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964

PRO_0000093708

Regions

Domain

95 – 153

CBS 1

Domain

157 – 216

CBS 2

Nucleotide binding

300 – 302

NAD By similarity

Region

340 – 342

IMP binding By similarity

Region

363 – 364

IMP binding By similarity

Region

387 – 391

IMP binding By similarity

Sites

Active site

307

Thioimidate intermediate By similarity

Metal binding

302

Potassium; via carbonyl oxygen By similarity

Metal binding

304

Potassium; via carbonyl oxygen By similarity

Metal binding

307

Potassium; via carbonyl oxygen By similarity

Metal binding

471

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

Metal binding

472

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

Metal binding

473

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

Binding site

250

NAD By similarity

Binding site

305

IMP By similarity

Binding site

417

IMP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P99106 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C4E945D25D41491D
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FASTA

488

52,851

        10         20         30         40         50         60 
MWESKFAKES LTFDDVLLIP AQSDILPKDV DLSVQLSDKV KLNIPVISAG MDTVTESKMA 

        70         80         90        100        110        120 
IAMARQGGLG VIHKNMGVEE QADEVQKVKR SENGVISNPF FLTPEESVYE AEALMGKYRI 

       130        140        150        160        170        180 
SGVPIVDNKE DRNLVGILTN RDLRFIEDFS IKIVDVMTQE NLITAPVNTT LEEAEKILQK 

       190        200        210        220        230        240 
HKIEKLPLVK DGRLEGLITI KDIEKVIEFP NAAKDEHGRL LVAAAIGISK DTDIRAQKLV 

       250        260        270        280        290        300 
EAGVDVLVID TAHGHSKGVI DQVKHIKKTY PEITLVAGNV ATAEATKDLF EAGADIVKVG 

       310        320        330        340        350        360 
IGPGSICTTR VVAGVGVPQI TAIYDCATEA RKHGKAIIAD GGIKFSGDII KALAAGGHAV 

       370        380        390        400        410        420 
MLGSLLAGTE ESPGATEIFQ GRQYKVYRGM GSLGAMEKGS NDRYFQEDKA PKKFVPEGIE 

       430        440        450        460        470        480 
GRTAYKGALQ DTIYQLMGGV RAGMGYTGSH DLRELREEAQ FTRMGPAGLA ESHPHNIQIT 


KESPNYSF

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315.
[2]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315.
[3]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB41602.1.
PIR	G89805.
RefSeq	NP_373624.1. NC_002745.2.
3D structure databases
ProteinModelPortal	P99106.
SMR	P99106. Positions 1-487.
ModBase	Search...
Protein-protein interaction databases
STRING	158879.SA0375.
2D gel databases
SWISS-2DPAGE	P99106.
Proteomic databases
PRIDE	P99106.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB41602; BAB41602; BAB41602.
GeneID	1123157.
KEGG	sau:SA0375.
PATRIC	19572814. VBIStaAur116463_0396.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0517.
HOGENOM	HOG000165754.
KO	K00088.
OMA	SAGLKES.
ProtClustDB	CLSK884611.
Enzyme and pathway databases
BioCyc	SAUR158879:GJCB-387-MONOMER.
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_STAAN

Accession

Primary (citable) accession number: P99106
Secondary accession number(s): Q99WI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 74 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

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel 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