Reviewed, UniProtKB/Swiss-Prot P49058 (IMDH_BORBU)

Names and origin

Protein names

Recommended name:
    Inosine-5'-monophosphate dehydrogenase
      Short name=IMP dehydrogenase
      Short name=IMPDH
      Short name=IMPD
    EC=1.1.1.205

Gene names

Name:	guaB
Ordered Locus Names:	BB_B17

Encoded on

Plasmid cp26 (circular 26 kb)

Organism

Borrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.
Pathway	Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Sequence similarities	Belongs to the IMPDH/GMPR family.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Ligand	Metal-binding NAD Potassium
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Plasmid
Gene Ontology (GO)
Biological process	GMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	IMP dehydrogenase activity Inferred from electronic annotation. Source: EC potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 404

404

Inosine-5'-monophosphate dehydrogenase

PRO_0000093692

Regions

Nucleotide binding

151 – 174

24

NAD By similarity

Sites

Active site

229

1

Thioimidate intermediate By similarity

Metal binding

224

1

Potassium; via carbonyl oxygen By similarity

Metal binding

226

1

Potassium; via carbonyl oxygen By similarity

Binding site

262

1

IMP By similarity

Binding site

309

1

IMP By similarity

Secondary structure

1

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404

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

12 – 14

3

Beta strand

15 – 17

3

Helix

26 – 28

3

Beta strand

33 – 38

6

Beta strand

40 – 47

8

Turn

51 – 53

3

Helix

56 – 65

10

Beta strand

67 – 71

5

Beta strand

73 – 75

3

Helix

77 – 88

12

Beta strand

145 – 148

4

Helix

154 – 163

10

Beta strand

167 – 171

5

Helix

179 – 191

13

Beta strand

196 – 202

7

Helix

205 – 212

8

Turn

213 – 215

3

Beta strand

217 – 221

5

Helix

230 – 235

6

Helix

241 – 252

12

Beta strand

258 – 263

6

Helix

268 – 277

10

Beta strand

280 – 284

5

Helix

286 – 289

4

Beta strand

294 – 296

3

Beta strand

298 – 301

4

Beta strand

304 – 307

4

Helix

352 – 370

19

Helix

375 – 380

6

Beta strand

384 – 387

4

Sequences

	Sequence		Length	Mass (Da)
	P49058-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: A91D6D6C5CE522F1	FASTA	404	43,768
	10 20 30 40 50 60 MPNKITKEAL TFDDVSLIPR KSSVLPSEVS LKTQLTKNIS LNIPFLSSAM DTVTESQMAI 70 80 90 100 110 120 AIAKEGGIGI IHKNMSIEAQ RKEIEKVKTY KFQKTINTNG DTNEQKPEIF TAKQHLEKSD 130 140 150 160 170 180 AYKNAEHKED FPNACKDLNN KLRVGAAVSI DIDTIERVEE LVKAHVDILV IDSAHGHSTR 190 200 210 220 230 240 IIELIKKIKT KYPNLDLIAG NIVTKEAALD LISVGADCLK VGIGPGSICT TRIVAGVGVP 250 260 270 280 290 300 QITAICDVYE ACNNTNICII ADGGIRFSGD VVKAIAAGAD SVMIGNLFAG TKESPSEEII 310 320 330 340 350 360 YNGKKFKSYV GMGSISAMKR GSKSRYFQLE NNEPKKLVPE GIEGMVPYSG KLKDILTQLK 370 380 390 400 GGLMSGMGYL GAATISDLKI NSKFVKISHS SLKESHPHDV FSIT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Plasmid location of Borrelia purine biosynthesis gene homologs." Margolis N., Hogan D., Tilly K., Rosa P. J. Bacteriol. 176:6427-6432(1994) [PubMed: 7961392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]	"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[3]	"Crystal structure at 2.4-A resolution of Borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6." McMillan F.M., Cahoon M., White A., Hedstrom L., Petsko G.A., Ringe D. Biochemistry 39:4533-4542(2000) [PubMed: 10758003] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

U13372 Genomic DNA. Translation: AAA53247.1.
AE000792 Genomic DNA. Translation: AAC66314.1.

PIR

E70218.

RefSeq

NP_047003.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EEP	X-ray	2.40	A/B	1-404	[»]

ModBase

Search...

Genome annotation databases

GeneID

1194400.

GenomeReviews

Gene locus BB_B17 in contig AE000792_GR.

KEGG

bbu:BBB17.

NMPDR

fig|224326.1.peg.1617.

TIGR

BB_B17.

Phylogenomic databases

HOGENOM

P49058.

OMA

P49058. CVGLITV.

Enzyme and pathway databases

BioCyc

BBUR224326:BB_B17-MON.

BRENDA

1.1.1.205. 142596.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF00478. IMPDH. 1 hit.
[Graphical view]

PROSITE

PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

IMDH_BORBU

Accession

Primary (citable) accession number: P49058

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)