ID K0ZZL9_9STRE Unreviewed; 328 AA.
AC K0ZZL9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=GMD4S_00440 {ECO:0000313|EMBL:EKA12191.1};
OS Streptococcus sp. GMD4S.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1169673 {ECO:0000313|EMBL:EKA12191.1, ECO:0000313|Proteomes:UP000004724};
RN [1] {ECO:0000313|EMBL:EKA12191.1, ECO:0000313|Proteomes:UP000004724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMD4S {ECO:0000313|EMBL:EKA12191.1,
RC ECO:0000313|Proteomes:UP000004724};
RX PubMed=23493677; DOI=10.1101/gr.142208.112;
RA Fitzsimons M.S., Novotny M., Lo C.C., Dichosa A.E., Yee-Greenbaum J.L.,
RA Snook J.P., Gu W., Chertkov O., Davenport K.W., McMurry K., Reitenga K.G.,
RA Daughton A.R., He J., Johnson S.L., Gleasner C.D., Wills P.L.,
RA Parson-Quintana B., Chain P.S., Detter J.C., Lasken R.S., Han C.S.;
RT "Nearly finished genomes produced using gel microdroplet culturing reveal
RT substantial intraspecies genomic diversity within the human microbiome.";
RL Genome Res. 23:878-888(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, 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:EKA12191.1}.
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DR EMBL; AJRE01000020; EKA12191.1; -; Genomic_DNA.
DR RefSeq; WP_000931181.1; NZ_AJRE01000020.1.
DR AlphaFoldDB; K0ZZL9; -.
DR PATRIC; fig|1169673.3.peg.75; -.
DR Proteomes; UP000004724; 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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01511}.
FT DOMAIN 9..311
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 176
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
FT BINDING 205..228
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
SQ SEQUENCE 328 AA; 35868 MW; 6EE3C1CA3066A300 CRC64;
MLNEFPIFDY EDIQLIPNKC VIKSRAEADT SVTLGNHTFK LPVVPANMQT ILDENVAEQL
AKGGYFYIMH RFDEAGRIPF IKRMHNQGLI ASISVGVKDY EYDFVSQLKA DAPEYITIDI
AHGHADSVIS MIQHIKKELP DTFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKV
KTGFGTGGWQ LAALRWCAKA ARKPIIADGG IRTHGDIAKS IRFGASMVMI GSLFAGHIES
PGKTIEVDGE QFKEYYGSAS QYQKGAYKNV EGKRILLPAK GHLQDTLTEM EQDLQSAISY
AGGRKVADLK HVDYVIVKNS IWNGDASH
//
