UniProtKB - P49058 (IMDH_BORBU)
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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
guaB
Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
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. Essential for mouse infection by tick bite and critical for the survival in environments that appear to lack sufficient amounts of guanine, guanosine, and/or deoxyguanosine to support spirochete growth, such as mammalian host tissues.2 Publications
Catalytic activityi
Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.1 Publication
Cofactori
K+1 Publication
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.By similarity
Kineticsi
- KM=29 µM for Inosine 5'-phosphate1 Publication
- KM=1100 µM for NAD+1 Publication
: XMP biosynthesis via de novo pathway Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.1 PublicationProteins known to be involved in this subpathway in this organism are:
- Inosine-5'-monophosphate dehydrogenase (guaB)
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 | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 172 | NADBy similarity | 1 | |
Metal bindingi | 224 | Potassium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 226 | Potassium; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 227 | IMPBy similarity | 1 | |
Active sitei | 229 | Thioimidate intermediateBy similarity | 1 | |
Metal bindingi | 229 | Potassium; via carbonyl oxygenBy similarity | 1 | |
Active sitei | 325 | Proton acceptorBy similarity | 1 | |
Binding sitei | 340 | IMPBy similarity | 1 | |
Metal bindingi | 394 | Potassium; via carbonyl oxygen; shared with tetrameric partnerBy similarity | 1 | |
Metal bindingi | 395 | Potassium; via carbonyl oxygen; shared with tetrameric partnerBy similarity | 1 | |
Metal bindingi | 396 | Potassium; via carbonyl oxygen; shared with tetrameric partnerBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 222 – 224 | NADBy similarity | 3 |
GO - Molecular functioni
- IMP dehydrogenase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- GMP biosynthetic process Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | GMP biosynthesis, Purine biosynthesis |
Ligand | Metal-binding, NAD, Potassium |
Enzyme and pathway databases
BRENDAi | 1.1.1.205. 902. |
UniPathwayi | UPA00601; UER00295. |
Names & Taxonomyi
Protein namesi | Recommended name: Inosine-5'-monophosphate dehydrogenase1 Publication (EC:1.1.1.2051 Publication)Short name: IMP dehydrogenase Short name: IMPD Short name: IMPDH1 Publication |
Gene namesi | Name:guaB1 Publication Ordered Locus Names:BB_B17 |
Encoded oni | Plasmid cp26 (circular 26 kb)0 Publication |
Organismi | Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) |
Taxonomic identifieri | 224326 [NCBI] |
Taxonomic lineagei | Bacteria › Spirochaetes › Spirochaetales › Borreliaceae › Borreliella › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000093692 | 2 – 404 | Inosine-5'-monophosphate dehydrogenaseAdd BLAST | 403 |
Proteomic databases
PRIDEi | P49058. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 12 – 14 | Combined sources | 3 | |
Beta strandi | 15 – 17 | Combined sources | 3 | |
Helixi | 26 – 28 | Combined sources | 3 | |
Beta strandi | 33 – 38 | Combined sources | 6 | |
Beta strandi | 40 – 47 | Combined sources | 8 | |
Turni | 51 – 53 | Combined sources | 3 | |
Helixi | 56 – 65 | Combined sources | 10 | |
Beta strandi | 67 – 71 | Combined sources | 5 | |
Beta strandi | 73 – 75 | Combined sources | 3 | |
Helixi | 77 – 88 | Combined sources | 12 | |
Beta strandi | 145 – 148 | Combined sources | 4 | |
Helixi | 154 – 163 | Combined sources | 10 | |
Beta strandi | 167 – 171 | Combined sources | 5 | |
Helixi | 179 – 191 | Combined sources | 13 | |
Beta strandi | 196 – 202 | Combined sources | 7 | |
Helixi | 205 – 212 | Combined sources | 8 | |
Turni | 213 – 215 | Combined sources | 3 | |
Beta strandi | 217 – 221 | Combined sources | 5 | |
Helixi | 230 – 235 | Combined sources | 6 | |
Helixi | 241 – 252 | Combined sources | 12 | |
Beta strandi | 258 – 263 | Combined sources | 6 | |
Helixi | 268 – 277 | Combined sources | 10 | |
Beta strandi | 280 – 284 | Combined sources | 5 | |
Helixi | 286 – 289 | Combined sources | 4 | |
Beta strandi | 294 – 296 | Combined sources | 3 | |
Beta strandi | 298 – 301 | Combined sources | 4 | |
Beta strandi | 304 – 307 | Combined sources | 4 | |
Helixi | 352 – 370 | Combined sources | 19 | |
Helixi | 375 – 380 | Combined sources | 6 | |
Beta strandi | 384 – 386 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EEP | X-ray | 2.40 | A/B | 1-404 | [»] | |
ProteinModelPortali | P49058. | |||||
SMRi | P49058. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P49058. |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 262 – 264 | IMP bindingBy similarity | 3 | |
Regioni | 285 – 286 | IMP bindingBy similarity | 2 | |
Regioni | 309 – 313 | IMP bindingBy similarity | 5 |
Sequence similaritiesi
Belongs to the IMPDH/GMPR family.Curated
Phylogenomic databases
KOi | K00088. |
OMAi | GIGIVHK. |
Family and domain databases
CDDi | cd00381. IMPDH. 1 hit. |
Gene3Di | 3.20.20.70. 2 hits. |
InterProi | View protein in InterPro IPR013785. Aldolase_TIM. IPR005990. IMP_DH. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. |
Pfami | View protein in Pfam PF00478. IMPDH. 1 hit. |
PIRSFi | PIRSF000130. IMPDH. 1 hit. |
PROSITEi | View protein in PROSITE PS00487. IMP_DH_GMP_RED. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P49058-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPNKITKEAL TFDDVSLIPR KSSVLPSEVS LKTQLTKNIS LNIPFLSSAM
60 70 80 90 100
DTVTESQMAI AIAKEGGIGI IHKNMSIEAQ RKEIEKVKTY KFQKTINTNG
110 120 130 140 150
DTNEQKPEIF TAKQHLEKSD AYKNAEHKED FPNACKDLNN KLRVGAAVSI
160 170 180 190 200
DIDTIERVEE LVKAHVDILV IDSAHGHSTR IIELIKKIKT KYPNLDLIAG
210 220 230 240 250
NIVTKEAALD LISVGADCLK VGIGPGSICT TRIVAGVGVP QITAICDVYE
260 270 280 290 300
ACNNTNICII ADGGIRFSGD VVKAIAAGAD SVMIGNLFAG TKESPSEEII
310 320 330 340 350
YNGKKFKSYV GMGSISAMKR GSKSRYFQLE NNEPKKLVPE GIEGMVPYSG
360 370 380 390 400
KLKDILTQLK GGLMSGMGYL GAATISDLKI NSKFVKISHS SLKESHPHDV
FSIT
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U13372 Genomic DNA. Translation: AAA53247.1. AE000792 Genomic DNA. Translation: AAC66314.1. |
PIRi | E70218. |
RefSeqi | NP_047003.1. NC_001903.1. WP_010890582.1. NC_001903.1. |
Genome annotation databases
EnsemblBacteriai | AAC66314; AAC66314; BB_B17. |
GeneIDi | 1194400. |
KEGGi | bbu:BB_B17. |
PATRICi | fig|224326.49.peg.1605. |
Similar proteinsi
Entry informationi
Entry namei | IMDH_BORBU | |
Accessioni | P49058Primary (citable) accession number: P49058 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1996 |
Last sequence update: | February 1, 1996 | |
Last modified: | February 28, 2018 | |
This is version 132 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |