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Database: UniProt
Entry: W0GLQ9_9MOLU
LinkDB: W0GLQ9_9MOLU
Original site: W0GLQ9_9MOLU 
ID   W0GLQ9_9MOLU            Unreviewed;       320 AA.
AC   W0GLQ9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=GMP reductase {ECO:0000256|ARBA:ARBA00015800};
DE            EC=1.7.1.7 {ECO:0000256|ARBA:ARBA00012678};
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|ARBA:ARBA00030699};
GN   ORFNames=P344_04605 {ECO:0000313|EMBL:AHI58243.1};
OS   Spiroplasma mirum ATCC 29335.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=838561 {ECO:0000313|EMBL:AHI58243.1, ECO:0000313|Proteomes:UP000019260};
RN   [1] {ECO:0000313|EMBL:AHI58243.1, ECO:0000313|Proteomes:UP000019260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMCA {ECO:0000313|EMBL:AHI58243.1,
RC   ECO:0000313|Proteomes:UP000019260};
RA   Landry C.A., Bastian F.O., Thune R.L.;
RT   "Complete genome sequence of Spiroplasma mirum suckling mouse cataract
RT   agent.";
RL   Submitted (SEP-2013) 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}.
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};
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DR   EMBL; CP006720; AHI58243.1; -; Genomic_DNA.
DR   RefSeq; WP_025317532.1; NZ_CP006720.1.
DR   AlphaFoldDB; W0GLQ9; -.
DR   STRING; 838561.P344_04605; -.
DR   KEGG; smia:P344_04605; -.
DR   KEGG; smir:SMM_0768; -.
DR   PATRIC; fig|838561.3.peg.880; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_0_14; -.
DR   OrthoDB; 9805398at2; -.
DR   Proteomes; UP000019260; Chromosome.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:InterPro.
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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AHI58243.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019260}.
FT   DOMAIN          4..309
FT                   /note="IMP dehydrogenase/GMP reductase"
FT                   /evidence="ECO:0000259|Pfam:PF00478"
SQ   SEQUENCE   320 AA;  35549 MW;  5369CA9CDAA82613 CRC64;
     MKAFDYEDIQ LIPKMCVVES RKECDPRVKL GKHTFNLPVV PSNMATVVNE ELCEKLAQQN
     YFYIMHRFNV DQVAFVKKMK QQGLIASISV GVKESDYQVI DNLKKENLTP DYITIDIAHA
     HALSVKKIIE HIRKNFKQAV FIIAGNVGTP KGVRDLEYWG ADATKVGIGP GKVCITKLKT
     GFGNGGWQLA AVKWCSKGSS KPIIADGGLR VNGDIAKSIR MGATMCMIGS LFAAHQESPG
     KLVVENGVEY KEYFGSASEY NKEEKRYVEG KKELITVRGS IFDTLKEMTE DLQSSISYAG
     GCDLEAIKKV DYVILKDSNF
//
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