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Q49729

- IMDH_MYCLE

UniProt

Q49729 - IMDH_MYCLE

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei283 – 2831NADUniRule annotation
Metal bindingi336 – 3361Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi338 – 3381Potassium; via carbonyl oxygenUniRule annotation
Binding sitei339 – 3391IMPUniRule annotation
Active sitei341 – 3411Thioimidate intermediateUniRule annotation
Metal bindingi341 – 3411Potassium; via carbonyl oxygenUniRule annotation
Binding sitei458 – 4581IMPUniRule annotation
Metal bindingi511 – 5111Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi512 – 5121Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi513 – 5131Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi334 – 3363NADUniRule annotation

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

UniPathwayiUPA00601; 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:ML0387
ORF Names:B1620_C3_238
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000806: Chromosome

Organism-specific databases

LepromaiML0387.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Inosine-5'-monophosphate dehydrogenasePRO_0000093701Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi272631.ML0387.

Structurei

3D structure databases

ProteinModelPortaliQ49729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 18557CBS 1UniRule annotationAdd
BLAST
Domaini189 – 24658CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni374 – 3763IMP bindingUniRule annotation
Regioni397 – 3982IMP bindingUniRule annotation
Regioni421 – 4255IMP bindingUniRule annotation

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 2 CBS domains.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165755.
KOiK00088.
OMAiHGHSKNI.
OrthoDBiEOG6GTZPV.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q49729-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIRGMSNLKE SSDFVASSYV RLGGLMDDPA ATGGDNPHKV AMLGLTFDDV
60 70 80 90 100
LLLPAASDVV PATADISSQL TKKIRLKVPL VSSAMDTVTE ARMAIAMARA
110 120 130 140 150
GGMGVLHRNL PVGEQAGQVE TVKRSEAGMV TDPVTCRPDN TLAQVGALCA
160 170 180 190 200
RFRISGLPVV DDSGALAGII TNRDMRFEVD QSKQVAEVMT KTPLITAAEG
210 220 230 240 250
VSADAALGLL RRNKIEKLPV VDGHGRLTGL ITVKDFVKTE QHPLATKDND
260 270 280 290 300
GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL IVDTAHAHNR LVLDMVGKLK
310 320 330 340 350
VEIGDRVQVI GGNVATRSAA AALVEAGADA VKVGVGPGST CTTRVVAGVG
360 370 380 390 400
APQITAILEA VAACGPAGVP VIADGGLQYS GDIAKALAAG ASTTMLGSLL
410 420 430 440 450
AGTAEAPGEL IFVNGKQFKS YRGMGSLGAM QGRGGDKSYS KDRYFADDAL
460 470 480 490 500
SEDKLVPEGI EGRVPFRGPL SSVIHQLVGG LRAAMGYTGS PTIEVLQQAQ
510 520
FVRITPAGLK ESHPHDVAMT VEAPNYYPR
Length:529
Mass (Da):54,814
Last modified:November 1, 1997 - v1
Checksum:i1565C62EC9529870
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00015 Genomic DNA. Translation: AAC43232.1.
AL583918 Genomic DNA. Translation: CAC29895.1.
PIRiS72823.
RefSeqiNP_301377.1. NC_002677.1.
WP_010907701.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC29895; CAC29895; CAC29895.
GeneIDi909092.
KEGGimle:ML0387.
PATRICi18051408. VBIMycLep78757_0653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00015 Genomic DNA. Translation: AAC43232.1 .
AL583918 Genomic DNA. Translation: CAC29895.1 .
PIRi S72823.
RefSeqi NP_301377.1. NC_002677.1.
WP_010907701.1. NC_002677.1.

3D structure databases

ProteinModelPortali Q49729.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272631.ML0387.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC29895 ; CAC29895 ; CAC29895 .
GeneIDi 909092.
KEGGi mle:ML0387.
PATRICi 18051408. VBIMycLep78757_0653.

Organism-specific databases

Lepromai ML0387.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165755.
KOi K00088.
OMAi HGHSKNI.
OrthoDBi EOG6GTZPV.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Smith D.R., Robison K.
    Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiIMDH_MYCLE
AccessioniPrimary (citable) accession number: Q49729
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3