ID   A0A091K2Y8_COLST        Unreviewed;       317 AA.
AC   A0A091K2Y8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 23.
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=N325_04995 {ECO:0000313|EMBL:KFP31837.1};
OS   Colius striatus (Speckled mousebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX   NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP31837.1, ECO:0000313|Proteomes:UP000053615};
RN   [1] {ECO:0000313|EMBL:KFP31837.1, ECO:0000313|Proteomes:UP000053615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP31837.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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|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; KK544281; KFP31837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091K2Y8; -.
DR   Proteomes; UP000053615; 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:SF3; GMP REDUCTASE 1; 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   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000235-3};
KW   Purine metabolism {ECO:0000256|ARBA:ARBA00022631};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053615}.
FT   DOMAIN          13..311
FT                   /note="IMP dehydrogenase/GMP reductase"
FT                   /evidence="ECO:0000259|Pfam:PF00478"
FT   ACT_SITE        158
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000235-1"
FT   BINDING         153
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000235-3"
FT   BINDING         155
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:KFP31837.1"
FT   NON_TER         317
FT                   /evidence="ECO:0000313|EMBL:KFP31837.1"
SQ   SEQUENCE   317 AA;  34127 MW;  4D70762D0A33EE73 CRC64;
     QVDLTRTFTF RNSKQTYTGI PIIVANMDTV GTFEMAVVMA KHAMFTAIHK HYSLEEWKLF
     AANHPECLEH VAASSGSGKA DLDKLTSILE AIPLIRYICL DVANGYSEHF VEFVKSVRAL
     FPHHTIMAGN VVTGEMVEEL ILSGADIIKV GIGPGSVCTT RIKTGVGYPQ LSAVIECADS
     AHGLKGHIIS DGGCSCPGDV AKAFGAGADF VMLGGMFAGH DQCAGEIMEK NGKKVKLFYG
     MSSDTAMKKH AGGVAEYRAS EGRTVEVPYR GDVELTILDI LGGLRSTCTY VGAAKLKELS
     RRTTFIRVTQ QHSQVFS
//