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Database: UniProt
Entry: C5T272_ACIDE
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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
//
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