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Database: UniProt
Entry: S5M1Y7_9MOLU
LinkDB: S5M1Y7_9MOLU
Original site: S5M1Y7_9MOLU 
ID   S5M1Y7_9MOLU            Unreviewed;       320 AA.
AC   S5M1Y7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
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   Name=guaC {ECO:0000313|EMBL:AGR42087.1};
GN   ORFNames=SDIMI_v3c03830 {ECO:0000313|EMBL:AGR42087.1};
OS   Spiroplasma diminutum CUAS-1.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=1276221 {ECO:0000313|EMBL:AGR42087.1, ECO:0000313|Proteomes:UP000014983};
RN   [1] {ECO:0000313|EMBL:AGR42087.1, ECO:0000313|Proteomes:UP000014983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CUAS-1 {ECO:0000313|EMBL:AGR42087.1};
RX   PubMed=23873917; DOI=10.1093/gbe/evt108;
RA   Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT   "Comparison of metabolic capacities and inference of gene content evolution
RT   in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL   Genome Biol. Evol. 5:1512-1523(2013).
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; CP005076; AGR42087.1; -; Genomic_DNA.
DR   RefSeq; WP_020836320.1; NC_021833.1.
DR   AlphaFoldDB; S5M1Y7; -.
DR   STRING; 1276221.SDIMI_v3c03830; -.
DR   KEGG; sdi:SDIMI_v3c03830; -.
DR   PATRIC; fig|1276221.3.peg.380; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_0_14; -.
DR   InParanoid; S5M1Y7; -.
DR   OrthoDB; 9805398at2; -.
DR   Proteomes; UP000014983; Chromosome.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000014983}.
FT   DOMAIN          4..313
FT                   /note="IMP dehydrogenase/GMP reductase"
FT                   /evidence="ECO:0000259|Pfam:PF00478"
SQ   SEQUENCE   320 AA;  35582 MW;  6AF0D56F7C24C0B6 CRC64;
     MYAFDYEDIQ LIPSMCVVNS RSECNTEVTL GKHTFKMPVM PANMASVINE ELCEMLARNG
     HFYVMHRFNV DSYAFTKKMN QENLISSISV GVKKEDYELI EKLANDNVVP DYITIDIAHG
     HSLSVKNMIE HIRKHMKNNT FIIAGNVGTP HAVRDLEFWG ADATKVGVGP GKVCITKLKT
     GFGTGGWQLG AIKWCSKASH KPIIADGGLR VNGDIAKSIR FGATMCMIGS LFAAHEESPG
     ANVTVDGVMF KEYYGSASEY NKGEKRYVEG KKELIKVRGK LMETYKEMQE DLQSSISYSG
     GTTLNDIKKV DYVILKTSNF
//
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