Reviewed, UniProtKB/Swiss-Prot P36959 (GMPR1_HUMAN)

Names and origin

Protein names

Recommended name:
    GMP reductase 1
    EC=1.7.1.7
Alternative name(s):
    Guanosine 5'-monophosphate oxidoreductase 1
      Short name=Guanosine monophosphate reductase 1

Gene names

Name:	GMPR
Synonyms:	GMPR1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Ref.6
Catalytic activity	Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH.
Subunit structure	Homotetramer.
Polymorphism	At least two different alleles are known.
Sequence similarities	Belongs to the IMPDH/GMPR family.
Caution	The N-terminus was initially (Ref.1) thought to be fused with glucose-6-phosphate-dehydrogenase (G6PD) protein in vivo. However, Ref.5 showed that it encodes a GMP reductase, and Ref.6 showed that the chimeric protein is an artifact.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Metal-binding NADP Potassium
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cold Traceable author statement. Source: ProtInc
Molecular function	GMP reductase activity Traceable author statement. Source: ProtInc 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 – 345

345

GMP reductase 1

PRO_0000093723

Regions

Nucleotide binding

108 – 131

24

NADP By similarity

Sites

Active site

186

1

Thioimidate intermediate By similarity

Metal binding

181

1

Potassium; via carbonyl oxygen By similarity

Metal binding

183

1

Potassium; via carbonyl oxygen By similarity

Binding site

219

1

NADP By similarity

Natural variations

Natural variant

234

1

A → T

VAR_003969

Natural variant

256

1

F → I: dbSNP rs1042391. Ref.4 Ref.8

VAR_003970

Secondary structure

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345

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Helix

12 – 14

3

Beta strand

15 – 17

3

Helix

27 – 29

3

Beta strand

34 – 37

4

Turn

39 – 41

3

Beta strand

44 – 47

4

Beta strand

50 – 52

3

Turn

56 – 58

3

Helix

61 – 67

7

Helix

68 – 70

3

Beta strand

73 – 75

3

Helix

82 – 91

10

Helix

93 – 98

6

Beta strand

99 – 103

5

Helix

107 – 119

13

Beta strand

125 – 129

5

Helix

136 – 148

13

Beta strand

152 – 159

8

Helix

162 – 170

9

Beta strand

174 – 178

5

Helix

188 – 191

4

Helix

198 – 210

13

Turn

211 – 213

3

Beta strand

215 – 220

6

Helix

225 – 234

10

Beta strand

237 – 242

6

Helix

243 – 245

3

Beta strand

251 – 253

3

Beta strand

263 – 267

5

Helix

272 – 277

6

Beta strand

285 – 288

4

Beta strand

292 – 296

5

Helix

301 – 319

19

Helix

324 – 326

3

Helix

327 – 330

4

Beta strand

332 – 337

6

Sequences

	Sequence		Length	Mass (Da)
	P36959-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 217E1A5A599CA510	FASTA	345	37,419
	10 20 30 40 50 60 MPRIDADLKL DFKDVLLRPK RSSLKSRAEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT 70 80 90 100 110 120 FEMAAVMSQH SMFTAIHKHY SLDDWKLFAT NHPECLQNVA VSSGSGQNDL EKMTSILEAV 130 140 150 160 170 180 PQVKFICLDV ANGYSEHFVE FVKLVRAKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV 190 200 210 220 230 240 GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM 250 260 270 280 290 300 LGGMFSGHTE CAGEVFERNG RKLKLFYGMS SDTAMNKHAG GVAEYRASEG KTVEVPYKGD 310 320 330 340 VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase." Kanno H., Huang I.Y., Kan Y.W., Yoshida A. Cell 58:595-606(1989) [PubMed: 2758468] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Genomic structure and expression of human guanosine monophosphate reductase." Kondoh T., Kanno H., Chang L., Yoshida A. Hum. Genet. 88:219-224(1991) [PubMed: 1661705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-256. Tissue: Placenta.
[5]	"The human mRNA that provides the N-terminus of chimeric G6PD encodes GMP reductase." Henikoff S., Smith J.M. Cell 58:1021-1022(1989) [PubMed: 2570640] [Abstract] Cited for: SIMILARITY TO GMP REDUCTASE.
[6]	"Origin of 'fused' glucose-6-phosphate dehydrogenase." Yoshida A., Kan Y.W. Cell 62:11-12(1990) [PubMed: 1694726] [Abstract] Cited for: LACK OF ROLE IN G6PD.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Identification of common variant alleles of the human guanosine monophosphate reductase gene." Kondoh T., Kanno H., Chang L., Yoshida A. Hum. Genet. 88:225-227(1991) [PubMed: 1757097] [Abstract] Cited for: VARIANTS THR-234 AND ILE-256.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L35304 Genomic DNA. Translation: AAA52503.1.
M27941 Genomic DNA. Translation: AAA53106.1.
M24470 mRNA. Translation: AAA52498.1.
AL009031, AL138883 Genomic DNA. Translation: CAI21422.1.
AL138883, AL009031 Genomic DNA. Translation: CAI19917.1.
BC008281 mRNA. Translation: AAH08281.1.

IPI

IPI00304803.

PIR

B32902.

RefSeq

NP_006868.3.

UniGene

Hs.484741

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BLE	X-ray	1.90	A	1-345	[»]
2BWG	X-ray	2.40	A/B/C/D	1-345	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P36959.

PTM databases

PhosphoSite

P36959.

Proteomic databases

PeptideAtlas

P36959.

PRIDE

P36959.

Genome annotation databases

Ensembl

ENST00000259727; ENSP00000259727; ENSG00000137198; Homo sapiens. [Genome view]

GeneID

2766.

KEGG

hsa:2766.

UCSC

uc003nbs.1. human.

Organism-specific databases

CTD

2766.

GeneCards

GC06P016346.

H-InvDB

HIX0005598.

HGNC

HGNC:4376. GMPR.

HPA

HPA000904.
HPA021476.

MIM

139265. gene.

PharmGKB

PA28761.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P36959.

HOVERGEN

P36959.

OMA

GRKLKLF.

Enzyme and pathway databases

BRENDA

1.7.1.7. 247.

Gene expression databases

ArrayExpress

P36959.

Bgee

P36959.

CleanEx

HS_GMPR.

Genevestigator

P36959.

GermOnline

ENSG00000137198. Homo sapiens.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR005993. GMP_reduct1.
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]

PIRSF

PIRSF000235. GMP_reductase. 1 hit.

TIGRFAMs

TIGR01305. GMP_reduct_1. 1 hit.

PROSITE

PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

10880.

SOURCE

Search...

Entry information

Entry name

GMPR1_HUMAN

Accession

Primary (citable) accession number: P36959
Secondary accession number(s): Q96HQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 3, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.