ID A0A195BME9_9HYME Unreviewed; 364 AA.
AC A0A195BME9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=GMP reductase {ECO:0000256|ARBA:ARBA00015800, ECO:0000256|RuleBase:RU003929};
DE EC=1.7.1.7 {ECO:0000256|ARBA:ARBA00012678, ECO:0000256|RuleBase:RU003929};
DE Flags: Fragment;
GN ORFNames=ALC53_04125 {ECO:0000313|EMBL:KYM86425.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM86425.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM86425.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM86425.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM86425.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica WGS genome.";
RL Submitted (SEP-2015) 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|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,
CC ECO:0000256|RuleBase:RU003929};
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DR EMBL; KQ976441; KYM86425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195BME9; -.
DR STRING; 520822.A0A195BME9; -.
DR Proteomes; UP000078540; Unassembled WGS sequence.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
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|PIRSR:PIRSR000235-3,
KW ECO:0000256|RuleBase:RU003929};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU003929};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000235-3};
KW Purine metabolism {ECO:0000256|ARBA:ARBA00022631};
KW Reference proteome {ECO:0000313|Proteomes:UP000078540}.
FT DOMAIN 14..352
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 190
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000235-1"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR000235-3"
FT BINDING 187
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR000235-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYM86425.1"
SQ SEQUENCE 364 AA; 39552 MW; C6356C7726DD66B3 CRC64;
RTAAMPNIIN DIKLDFKDVL LRPKRSTLKS RSDVDLFREI TFRNSKQTYR GIPVMASNMD
TIGTFEMAKA LSKHGLFTTV HKYYTADEWK DFIALNPDCA KNVAATSGTG KEDYERLSSI
LEVVPELSFI CLDVANGYSQ HFVEYVRKVR ARYPNHTIIA GNVVTGEMVE ELILSGADII
KVGIGPGSVC TTRMKTGVGF PQLSAVIECA DAAHGLKGHI IADGGCTCPG DLAKAFGGGA
DFVMAGGIFA GHDECGGEVI EKNGKKFKLF YGMSSNTAML KHAGGVADYR KSSVLISMHR
SSEGKTVEVP YKGLVENTVL DILGGLRSAC TYIGAQRLRE LPRRATFIRC TQQLNPLYGP
PPVI
//
