GUAC_ACIAC
ID GUAC_ACIAC Reviewed; 325 AA.
AC A1TNF7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_01511};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE Short=Guanosine monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_01511};
GN Name=guaC {ECO:0000255|HAMAP-Rule:MF_01511}; OrderedLocusNames=Aave_1911;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP
CC to IMP. It functions in the conversion of nucleobase, nucleoside and
CC nucleotide derivatives of G to A nucleotides, and in maintaining the
CC intracellular balance of A and G nucleotides. {ECO:0000255|HAMAP-
CC Rule:MF_01511}.
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:0000255|HAMAP-
CC Rule:MF_01511};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01511}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000512; ABM32495.1; -; Genomic_DNA.
DR RefSeq; WP_011795038.1; NC_008752.1.
DR AlphaFoldDB; A1TNF7; -.
DR SMR; A1TNF7; -.
DR STRING; 397945.Aave_1911; -.
DR EnsemblBacteria; ABM32495; ABM32495; Aave_1911.
DR KEGG; aav:Aave_1911; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_5_0_4; -.
DR OMA; AYKEYFG; -.
DR OrthoDB; 532857at2; -.
DR Proteomes; UP000002596; 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:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01511; GMP_reduct_type2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005994; GuaC_type_2.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF036500; GMP_red_Firmic; 1.
DR TIGRFAMs; TIGR01306; GMP_reduct_2; 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..325
FT /note="GMP reductase"
FT /id="PRO_0000294269"
FT ACT_SITE 173
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT BINDING 202..225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
SQ SEQUENCE 325 AA; 35753 MW; 87BEE0C1DC2B1FE4 CRC64;
MEIFDYDNVL LLPRKCRVES RSECDASVTL GQRSFRLPVV PANMKTVVDE KICRWLASNG
YFYVMHRFDL DNVQFVRDMH AAGCFASISL GVKQPDYDTV DRLVAEGLCP EYITIDIAHG
HADTVKAMIA YLKQHLPQAF VIAGNVATPE AIIDLENWGA DATKVGVGPG KVCITKLKTG
FGTGGWQLSA LKWCARVATK PIIADGGIRS HGDIAKSIRF GATMVMIGSL FAGHEESPGK
TVEVDGEQFK EYYGSASDFN KGEYKHVEGK RILEPIKGRL ADTLVEMEQD VQSSISYSGG
RRLMDIRKVN YVILGGDNAG EHLLM
