(data stored in SCRATCH zone)

SWISSPROT: C8U1H5_ECO10

ID   C8U1H5_ECO10            Unreviewed;       347 AA.
AC   C8U1H5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=GMP reductase {ECO:0000256|HAMAP-Rule:MF_00596};
DE            EC=1.7.1.7 {ECO:0000256|HAMAP-Rule:MF_00596};
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00596};
DE            Short=Guanosine monophosphate reductase {ECO:0000256|HAMAP-Rule:MF_00596};
GN   Name=guaC {ECO:0000256|HAMAP-Rule:MF_00596,
GN   ECO:0000313|EMBL:BAI28983.1};
GN   OrderedLocusNames=ECO103_0105 {ECO:0000313|EMBL:BAI28983.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28983.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28983.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination
CC       of GMP to IMP. It functions in the conversion of nucleobase,
CC       nucleoside and nucleotide derivatives of G to A nucleotides, and
CC       in maintaining the intracellular balance of A and G nucleotides.
CC       {ECO:0000256|HAMAP-Rule:MF_00596, ECO:0000256|RuleBase:RU003929,
CC       ECO:0000256|SAAS:SAAS00825629}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC         Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00596, ECO:0000256|RuleBase:RU003929,
CC         ECO:0000256|SAAS:SAAS01120721};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00596}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00596}.
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DR   EMBL; AP010958; BAI28983.1; -; Genomic_DNA.
DR   RefSeq; WP_001217338.1; NC_013353.1.
DR   SMR; C8U1H5; -.
DR   EnsemblBacteria; BAI28983; BAI28983; ECO103_0105.
DR   KEGG; eoh:ECO103_0105; -.
DR   HOGENOM; HOG000165756; -.
DR   KO; K00364; -.
DR   OMA; AYKEYFG; -.
DR   BioCyc; ECOL585395:ECO103_RS00535-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00596; GMP_reduct_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005993; GMPR.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000235; GMP_reductase; 1.
DR   TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1H5.
DR   SWISS-2DPAGE; C8U1H5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00596,
KW   ECO:0000256|PIRSR:PIRSR000235-3, ECO:0000256|RuleBase:RU003929,
KW   ECO:0000256|SAAS:SAAS00765560};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00596, ECO:0000256|RuleBase:RU003929,
KW   ECO:0000256|SAAS:SAAS00825633};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00596,
KW   ECO:0000256|SAAS:SAAS00765563};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_00596,
KW   ECO:0000256|PIRSR:PIRSR000235-3, ECO:0000256|RuleBase:RU003929,
KW   ECO:0000256|SAAS:SAAS00765562}.
FT   DOMAIN        9    338       IMPDH. {ECO:0000259|Pfam:PF00478}.
FT   NP_BIND     108    131       NADP. {ECO:0000256|HAMAP-Rule:MF_00596}.
FT   NP_BIND     216    239       NADP; ribose moiety. {ECO:0000256|HAMAP-
FT                                Rule:MF_00596}.
FT   ACT_SITE    186    186       Thioimidate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00596,
FT                                ECO:0000256|PIRSR:PIRSR000235-1}.
FT   METAL       181    181       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00596,
FT                                ECO:0000256|PIRSR:PIRSR000235-3}.
FT   METAL       183    183       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00596,
FT                                ECO:0000256|PIRSR:PIRSR000235-3}.
SQ   SEQUENCE   347 AA;  37384 MW;  898F50DA7FD00441 CRC64;
     MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII AANMDTVGTF
     SMASALASFD ILTAVHKHYS VEEWQAFINN SSADVLKHVM VSTGTSDADF EKTKQILDLN
     PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI
     GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM
     LGGMLAGHEE SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP
     VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL
//

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