SWISSPROT: Q13DJ7_RHOPS

ID   Q13DJ7_RHOPS            Unreviewed;       347 AA.
AC   Q13DJ7;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 84.
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   OrderedLocusNames=RPD_0604 {ECO:0000313|EMBL:ABE37842.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37842.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37842.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37842.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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|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|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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00596}.
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DR   EMBL; CP000283; ABE37842.1; -; Genomic_DNA.
DR   RefSeq; WP_011501029.1; NC_007958.1.
DR   STRING; 316057.RPD_0604; -.
DR   EnsemblBacteria; ABE37842; ABE37842; RPD_0604.
DR   KEGG; rpd:RPD_0604; -.
DR   eggNOG; ENOG4105CP4; Bacteria.
DR   eggNOG; COG0516; LUCA.
DR   HOGENOM; HOG000165756; -.
DR   KO; K00364; -.
DR   OMA; AYKEYFG; -.
DR   OrthoDB; 532857at2; -.
DR   BioCyc; RPAL316057:RPD_RS03100-MONOMER; -.
DR   Proteomes; UP000001818; 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   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13DJ7.
DR   SWISS-2DPAGE; Q13DJ7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00596,
KW   ECO:0000256|PIRSR:PIRSR000235-3};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00596, ECO:0000256|SAAS:SAAS00825633};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00596};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_00596,
KW   ECO:0000256|PIRSR:PIRSR000235-3}.
FT   DOMAIN        9    338       IMPDH. {ECO:0000259|Pfam:PF00478}.
FT   NP_BIND     212    235       NADP; ribose moiety. {ECO:0000256|HAMAP-
FT                                Rule:MF_00596}.
FT   ACT_SITE    182    182       Thioimidate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00596,
FT                                ECO:0000256|PIRSR:PIRSR000235-1}.
FT   METAL       177    177       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00596,
FT                                ECO:0000256|PIRSR:PIRSR000235-3}.
FT   METAL       179    179       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00596,
FT                                ECO:0000256|PIRSR:PIRSR000235-3}.
SQ   SEQUENCE   347 AA;  37477 MW;  1118CADA631EB666 CRC64;
     MHIDLNPKLD FRDVLIRPKR SVLASRFEAN ISRTFGFRHS SREWTGFPLI ASNMDTIGTL
     EMADAFRPFG ALVALHKFYD PERLAKYLDD HANPNVFLTV GTGASDWDRL AAVKKQTKVP
     VLNIDVANGY TENFVRAVSK LREENPDAII MAGTVVTAEM TEALVIAGAD IVRVGIGSGS
     VCTTRDLTGV GYPQLSAVIE CADAAHGLKG HVCSDGGCTV PGDVAKAYGG GADFVMLGGM
     LAGHVECGGE LRYLEEGGKR VPKSMVFYGM SSETAMNKYH GGVADYRAAE GKTVEVPYRG
     EVRATVETIA GGLRSAMTYM GAENLKEIPK RTTFILVNAQ RNTVFDR
//