P65168 (IMDH_MYCBO) Reviewed, UniProtKB/Swiss-Prot

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:	Mb3445c

Organism

Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]

Taxonomic identifier

233413 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. HAMAP-Rule MF_01964
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. HAMAP-Rule MF_01964
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: UniProtKB-HAMAP
Molecular_function	IMP dehydrogenase activity Inferred from electronic annotation. Source: UniProtKB-HAMAP adenyl nucleotide binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-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_0000093700
Regions
	Domain	129 – 185	57	CBS 1
	Domain	189 – 246	58	CBS 2
	Nucleotide binding	334 – 336	3	NAD By similarity
	Region	374 – 376	3	IMP binding By similarity
	Region	397 – 398	2	IMP binding By similarity
	Region	421 – 425	5	IMP binding By similarity
Sites
	Active site	341	1	Thioimidate intermediate By similarity
	Metal binding	336	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	338	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	341	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	511	1	Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
	Metal binding	512	1	Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
	Metal binding	513	1	Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
	Binding site	283	1	NAD By similarity
	Binding site	339	1	IMP By similarity
	Binding site	458	1	IMP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P65168 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 689A7C7C53993C0A	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

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. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248333 Genomic DNA. Translation: CDO44716.1.
RefSeq	NP_857085.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P65168.
SMR	P65168. Positions 6-526.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	233413.Mb3445c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD95632; CAD95632; Mb3445c.
GeneID	1091016.
KEGG	mbo:Mb3445c.
PATRIC	18009304. VBIMycBov88188_3780.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0517.
HOGENOM	HOG000165755.
KO	K00088.
OMA	FQADVRS.
OrthoDB	EOG6GTZPV.
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. CBS_dom. IPR005990. IMP_DH. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. [Graphical view]
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_MYCBO

Accession

Primary (citable) accession number: P65168
Secondary accession number(s): Q50715, X2BPI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 11, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program