ID GUAC_BUCAI Reviewed; 349 AA.
AC P57300;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=GMP reductase;
DE EC=1.7.1.7;
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase;
DE Short=Guanosine monophosphate reductase;
GN Name=guaC; OrderedLocusNames=BU204;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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 (By similarity).
CC {ECO:0000250}.
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;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BA000003; BAB12921.1; -; Genomic_DNA.
DR RefSeq; NP_240035.1; NC_002528.1.
DR RefSeq; WP_009874161.1; NC_002528.1.
DR AlphaFoldDB; P57300; -.
DR SMR; P57300; -.
DR STRING; 563178.BUAP5A_201; -.
DR EnsemblBacteria; BAB12921; BAB12921; BAB12921.
DR KEGG; buc:BU204; -.
DR PATRIC; fig|107806.10.peg.215; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_5_3_6; -.
DR Proteomes; UP000001806; 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; Aldolase class I; 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 NCBIfam; TIGR01305; GMP_reduct_1; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW Metal-binding; NADP; Oxidoreductase; Potassium; Reference proteome.
FT CHAIN 1..349
FT /note="GMP reductase"
FT /id="PRO_0000093732"
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 108..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 216..239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 38320 MW; D4D109BD6B493D72 CRC64;
MRIEEDIKLG FKDVLIRPKR SILKSRSQVN LARCFSFKYS ASIWSGIPII AANMDTIGTF
EMVKSLSKFN ILTAVHKYYS FEEWKNFVCL SSKEILNHVI VSIGTSNIDF LKIKKIFLLS
SELKYICIDV ANGYSEHIVS FLKLVRDYFP DKIICAGNVV TGEMVEELIL SGADIVKVGI
GPGSVCTTRV KTGVGYPQLS AIIECADAAH GLNGQIISDG GCTVSGDIAK AFGGGADFVM
LGGMLSGHKE CSGDIIEEKS KKYMIFYGMS SVSAMQRYEG KIAGYRASEG KTVKIPFRGG
VDSTIRDILG GLRSSCTYVG AEKLKELTKR TTFIRVTEQE NCIFNAFKE
//
