ID C5T272_ACIDE Unreviewed; 325 AA.
AC C5T272;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=GMP reductase {ECO:0000256|HAMAP-Rule:MF_01511};
DE EC=1.7.1.7 {ECO:0000256|HAMAP-Rule:MF_01511};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01511};
DE Short=Guanosine monophosphate reductase {ECO:0000256|HAMAP-Rule:MF_01511};
GN Name=guaC {ECO:0000256|HAMAP-Rule:MF_01511};
GN ORFNames=AcdelDRAFT_1002 {ECO:0000313|EMBL:EER61413.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER61413.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER61413.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER61413.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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.
CC {ECO:0000256|ARBA:ARBA00037691, ECO:0000256|HAMAP-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;
CC Evidence={ECO:0000256|ARBA:ARBA00000930, ECO:0000256|HAMAP-
CC Rule:MF_01511};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01511}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EER61413.1}.
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DR EMBL; ACQT01000017; EER61413.1; -; Genomic_DNA.
DR RefSeq; WP_005794022.1; NZ_ACQT01000017.1.
DR AlphaFoldDB; C5T272; -.
DR PATRIC; fig|573060.9.peg.4173; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000003856; Unassembled WGS sequence.
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; Aldolase class I; 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 NCBIfam; TIGR01306; GMP_reduct_2; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF036500; GMP_red_Firmic; 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 NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01511};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01511};
KW Reference proteome {ECO:0000313|Proteomes:UP000003856}.
FT DOMAIN 5..308
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 173
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
FT BINDING 202..225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
SQ SEQUENCE 325 AA; 35602 MW; 5F09D69DC8AD85A7 CRC64;
MEIFDYDNIL LLPRKCRVES RSECDASVEL GGRSFRIPVV PANMKTVVDE KICTWLAQNG
YFYVMHRFDL DNLQFVKDMH AKGCYASISL GVKAPDYATV DQLVAQGITP EYITIDIAHG
HADSVKNMIT YLKDKLPRAF VIAGNVATPE AIIDLENWGA DATKVGVGPG KVCITKLKTG
FGTGGWQLSA LKWCARVATK PIIADGGIRS HGDIAKSIRF GATMVMIGSL FAGHEESPGK
TVEVDGELFK EYYGSASDFN KGEYKHVEGK RILEPIKGRL AETLIEMEQD VQSSISYAGG
TKLMDVRKVN YVILGGDNAG EHLLM
//