guaB

Functionⁱ

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.UniRule annotation

Catalytic activityⁱ

Inosine 5'-phosphate + NAD⁺ + H₂O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactorⁱ

K⁺UniRule annotation

Enzyme regulationⁱ

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.UniRule annotation

Pathwayⁱ: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:

Inosine-5'-monophosphate dehydrogenase (guaB)

This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	283	NADUniRule annotation	1
Metal bindingⁱ	336	Potassium; via carbonyl oxygenUniRule annotation	1
Metal bindingⁱ	338	Potassium; via carbonyl oxygenUniRule annotation	1
Binding siteⁱ	339	IMPUniRule annotation	1
Active siteⁱ	341	Thioimidate intermediateUniRule annotation	1
Metal bindingⁱ	341	Potassium; via carbonyl oxygenUniRule annotation	1
Active siteⁱ	443	Proton acceptorUniRule annotation	1
Binding siteⁱ	458	IMPUniRule annotation	1
Metal bindingⁱ	511	Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation	1
Metal bindingⁱ	512	Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation	1
Metal bindingⁱ	513	Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	334 – 336	NADUniRule annotation		3

GO - Molecular functionⁱ

IMP dehydrogenase activity Source: UniProtKB-EC
metal ion binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

GMP biosynthetic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	GMP biosynthesis, Purine biosynthesis
Ligand	Metal-binding, NAD, Potassium

Enzyme and pathway databases

BioCycⁱ	MBOV233413:G1GT4-3620-MONOMER
UniPathwayⁱ	UPA00601; UER00295

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation) Short name: IMP dehydrogenaseUniRule annotation Short name: IMPDUniRule annotation Short name: IMPDHUniRule annotation
Gene namesⁱ	Name:guaBUniRule annotation Ordered Locus Names:BQ2027_MB3445C
Organismⁱ	Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifierⁱ	233413 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Actinobacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis
Proteomesⁱ	UP000001419 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000093700	1 – 529	Inosine-5'-monophosphate dehydrogenaseAdd BLAST		529

Interactionⁱ

Subunit structureⁱ

Homotetramer.UniRule annotation

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P65168
SMRⁱ	P65168
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	129 – 185	CBS 1UniRule annotationAdd BLAST		57
Domainⁱ	189 – 246	CBS 2UniRule annotationAdd BLAST		58

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	374 – 376	IMP bindingUniRule annotation	3
Regionⁱ	397 – 398	IMP bindingUniRule annotation	2
Regionⁱ	421 – 425	IMP bindingUniRule annotation	5

Sequence similaritiesⁱ

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domainⁱ

CBS domain, Repeat

Phylogenomic databases

HOGENOMⁱ	HOG000165755
OMAⁱ	GIGIVHK

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00381 IMPDH, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
HAMAPⁱ	MF_01964 IMPDH, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR000644 CBS_dom IPR005990 IMP_DH IPR015875 IMP_DH/GMP_Rdtase_CS IPR001093 IMP_DH_GMPRt
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00571 CBS, 2 hits PF00478 IMPDH, 1 hit
PIRSFⁱ	PIRSF000130 IMPDH, 1 hit
SMARTⁱ	View protein in SMART SM00116 CBS, 2 hits
TIGRFAMsⁱ	TIGR01302 IMP_dehydrog, 1 hit
PROSITEⁱ	View protein in PROSITE PS51371 CBS, 2 hits PS00487 IMP_DH_GMP_RED, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P65168-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSRGMSGLED SSDLVVSPYV RMGGLTTDPV PTGGDDPHKV AMLGLTFDDV 
        60         70         80         90        100
LLLPAASDVV PATADTSSQL TKKIRLKVPL VSSAMDTVTE SRMAIAMARA 
       110        120        130        140        150
GGMGVLHRNL PVAEQAGQVE MVKRSEAGMV TDPVTCRPDN TLAQVDALCA 
       160        170        180        190        200
RFRISGLPVV DDDGALVGII TNRDMRFEVD QSKQVAEVMT KAPLITAQEG 
       210        220        230        240        250
VSASAALGLL RRNKIEKLPV VDGRGRLTGL ITVKDFVKTE QHPLATKDSD 
       260        270        280        290        300
GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL VVDTAHAHNR LVLDMVGKLK 
       310        320        330        340        350
SEVGDRVEVV GGNVATRSAA AALVDAGADA VKVGVGPGSI CTTRVVAGVG 
       360        370        380        390        400
APQITAILEA VAACRPAGVP VIADGGLQYS GDIAKALAAG ASTAMLGSLL 
       410        420        430        440        450
AGTAEAPGEL IFVNGKQYKS YRGMGSLGAM RGRGGATSYS KDRYFADDAL 
       460        470        480        490        500
SEDKLVPEGI EGRVPFRGPL SSVIHQLTGG LRAAMGYTGS PTIEVLQQAQ 
       510        520 
FVRITPAGLK ESHPHDVAMT VEAPNYYAR

Length:529

Mass (Da):54,867

Last modified:October 11, 2004 - v1

Checksum:ⁱ689A7C7C53993C0A

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	LT708304 Genomic DNA Translation: SIU02073.1
NCBI Reference Sequences More...RefSeqⁱ	NP_857085.1, NC_002945.3 WP_003900682.1, NC_002945.4

Genome annotation databases

EnsemblBacteriaⁱ	CDO44716; CDO44716; Mb3445c
PATRICⁱ	fig\|233413.5.peg.3780

Protein	Similar proteins		Species	Score	Length
P65168	Inosine-5'-monophosphate dehydrogenase		MYCLE		529
Inosine-5'-monophosphate dehydrogenase		Mycobacterium leprae 3125609		529
Inosine-5'-monophosphate dehydrogenase		MYCLB		529
Inosine-5'-monophosphate dehydrogenase		MYCKA		539
Inosine-5'-monophosphate dehydrogenase		Mycobacterium sp. 1081908.1		537
+262

Protein	Similar proteins		Species	Score	Length
P65168	Inosine-5'-monophosphate dehydrogenase		MYCLE		529
Inosine-5'-monophosphate dehydrogenase		Mycobacterium leprae 3125609		529
Inosine-5'-monophosphate dehydrogenase		MYCLB		529
Inosine-5'-monophosphate dehydrogenase		MYCKA		539
Inosine-5'-monophosphate dehydrogenase		Mycobacterium kansasii ATCC 12478		537
+750

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	LT708304 Genomic DNA Translation: SIU02073.1
NCBI Reference Sequences More...RefSeqⁱ	NP_857085.1, NC_002945.3 WP_003900682.1, NC_002945.4

3D structure databases

ProteinModelPortalⁱ	P65168
SMRⁱ	P65168
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	CDO44716; CDO44716; Mb3445c
PATRICⁱ	fig\|233413.5.peg.3780

Phylogenomic databases

HOGENOMⁱ	HOG000165755
OMAⁱ	GIGIVHK

Enzyme and pathway databases

UniPathwayⁱ	UPA00601; UER00295
BioCycⁱ	MBOV233413:G1GT4-3620-MONOMER

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00381 IMPDH, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
HAMAPⁱ	MF_01964 IMPDH, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR000644 CBS_dom IPR005990 IMP_DH IPR015875 IMP_DH/GMP_Rdtase_CS IPR001093 IMP_DH_GMPRt
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00571 CBS, 2 hits PF00478 IMPDH, 1 hit
PIRSFⁱ	PIRSF000130 IMPDH, 1 hit
SMARTⁱ	View protein in SMART SM00116 CBS, 2 hits
TIGRFAMsⁱ	TIGR01302 IMP_dehydrog, 1 hit
PROSITEⁱ	View protein in PROSITE PS51371 CBS, 2 hits PS00487 IMP_DH_GMP_RED, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	IMDH_MYCBO
Accessionⁱ	P65168Primary (citable) accession number: P65168 Secondary accession number(s): A0A1R3Y452, Q50715, X2BPI0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
	Last sequence update:	October 11, 2004
	Last modified:	April 25, 2018
	This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P65168 (IMDH_MYCBO)

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Inosine-5'-monophosphate dehydrogenase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: XMP biosynthesis via de novo pathway

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Enzyme regulationⁱ

Pathwayⁱ: XMP biosynthesis via de novo pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ