ID A0A081NJL6_9GAMM Unreviewed; 345 AA.
AC A0A081NJL6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=GZ78_00450 {ECO:0000313|EMBL:KEQ18639.1};
OS Endozoicomonas numazuensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=1137799 {ECO:0000313|EMBL:KEQ18639.1, ECO:0000313|Proteomes:UP000028073};
RN [1] {ECO:0000313|EMBL:KEQ18639.1, ECO:0000313|Proteomes:UP000028073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25634 {ECO:0000313|EMBL:KEQ18639.1,
RC ECO:0000313|Proteomes:UP000028073};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) 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_00596,
CC ECO:0000256|RuleBase:RU003929}.
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_00596, ECO:0000256|RuleBase:RU003929};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00596}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00596}.
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:KEQ18639.1}.
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DR EMBL; JOKH01000001; KEQ18639.1; -; Genomic_DNA.
DR RefSeq; WP_034831874.1; NZ_JOKH01000001.1.
DR AlphaFoldDB; A0A081NJL6; -.
DR STRING; 1137799.GZ78_00450; -.
DR eggNOG; COG0516; Bacteria.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000028073; 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: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; Aldolase class I; 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 NCBIfam; TIGR01305; GMP_reduct_1; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 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 Metal-binding {ECO:0000256|HAMAP-Rule:MF_00596,
KW ECO:0000256|PIRSR:PIRSR000235-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00596};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00596};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00596};
KW Reference proteome {ECO:0000313|Proteomes:UP000028073}.
FT DOMAIN 9..338
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-1"
FT BINDING 108..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-3"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-3"
FT BINDING 216..239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596"
SQ SEQUENCE 345 AA; 37313 MW; C165A6596E9AD872 CRC64;
MRVEADIKLG FKDVLFRPKR STLKSRSQVS LERTFKFVHT DQEWTGVPVI AANMDTVGTF
SIALALAEHK MLTAVHKHYT IEEWKAFLDS APAGIENHIM VSSGTSEADF VKLNDILALD
DKLRFICIDV ANGYSEHFVQ YVSKVRKQHP GKVIIAGNVV TGEMVEELIL KGADIVKVGI
GPGSVCTTRV KTGVGYPQLS ATIECADAAH GVGGQIISDG GCTCAGDVSK AFGGGADFVM
IGGMFAGHDE SAGEEVEEDG KKFKLFYGMS SETAMDKHSG GVANYRASEG KTVKVPYRGP
VENTVQDILG GVRSTCTYVG AATLKELTKR TTFIRVQEQE NRFFN
//
