NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
DOI=10.1093/nar/gkf526; PubMed=12235376 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Takaki Y., Uchiyama I.;
"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments.";
Nucleic Acids Res. 30:3927-3935(2002).

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 (By similarity).
CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH₃ + NADP⁺ = guanosine 5'-phosphate + NADPH.
SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000028; BAC13266.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_692231.1; -.

3D structure databases

HSSP

P12268; 1B3O. [HSSP ENTRY / PDB]

SMR

Q8ERJ2; 3-320.

ModBase

Q8ERJ2.

Enzyme and pathway databases

BioCyc

OIHE221109:OB1310-MON; -.

Ontologies

GO:0003920;	Molecular function: GMP reductase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
GO:0006163;	Biological process: purine nucleotide metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01511; -; 1.
PBIL [Tree]

InterPro

IPR013785; Aldolase_TIM.
IPR005994; GMP_reduct2.
IPR015875; IMP_DH/GMP_Rdtase_CS.
IPR001093; IMP_DHase_GMPRtase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF00478; IMPDH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036500; GMP_red_Firmic; 1.

TIGRFAMs

TIGR01306; GMP_reduct_2; 1.

PROSITE

PS00487; IMP_DH_GMP_RED; 1.

Genome annotation databases

1017488; -.

BA000028_GR; OB1310.

oih:OB1310; -.

fig|221109.1.peg.1314; -.

Phylogenomic databases

HOGENOM

Q8ERJ2; -.

Genome annotation databases

CMR

Q8ERJ2; OB1310.

Other

ProtoNet

Q8ERJ2.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 327`	`327`	`GMP reductase.`	`PRO_0000093762`
`NP_BIND`	`204 227`	`24`	`NADP (By similarity).`
`ACT_SITE`	`175 175`		`Thioimidate intermediate (By similarity).`

Sequence information

Length: 327 AA [This is the length of the unprocessed precursor]

Molecular weight: 36203 Da [This is the MW of the unprocessed precursor]

CRC64: F10D02B8A546BAEE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MENVFDYEDI QLIPAKCVVN SRSECDTSVT LGNRTFKLPV VPANMQTIID EKIAKYLAEK 

        70         80         90        100        110        120 
NYFYIMHRFE PEKRIDFIQD MQEYNLFTSI SVGVKEEEYT FIEDLAAKQL IPDYITIDIA 

       130        140        150        160        170        180 
HGHSDAVIKM IKHIKNNLPS SFVIAGNVGT PEAVRELENA GADATKVGIG PGKVCITKIK 

       190        200        210        220        230        240 
TGFGTGGWQL AALRWCAKAA SKPIIADGGI RTHGDIAKSI RFGASMVMIG SLFAGHEESP 

       250        260        270        280        290        300 
GETIEQDGKK IKEYFGSASE FQKGEKKNVE GKKMYVEHKG PLQDTLTEME QDLQSSISYA 

       310        320 
GGKQLDAIRN VDYVVVKNSI FNGDKVF

Q8ERJ2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools