ID A0A6H5GQU0_9HEMI Unreviewed; 545 AA.
AC A0A6H5GQU0;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=IMP dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=NTEN_LOCUS11904 {ECO:0000313|EMBL:CAB0006427.1};
OS Nesidiocoris tenuis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Miridae; Dicyphina; Nesidiocoris.
OX NCBI_TaxID=355587 {ECO:0000313|EMBL:CAB0006427.1, ECO:0000313|Proteomes:UP000479000};
RN [1] {ECO:0000313|EMBL:CAB0006427.1, ECO:0000313|Proteomes:UP000479000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ferguson B K.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+); Xref=Rhea:RHEA:11708,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053;
CC EC=1.1.1.205; Evidence={ECO:0000256|ARBA:ARBA00048028};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC {ECO:0000256|ARBA:ARBA00005502}.
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DR EMBL; CADCXU010017654; CAB0006427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6H5GQU0; -.
DR OrthoDB; 416622at2759; -.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000479000; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:TreeGrafter.
DR CDD; cd04601; CBS_pair_IMPDH; 1.
DR CDD; cd00381; IMPDH; 1.
DR CDD; cd13314; PH_Rpn13; 1.
DR FunFam; 3.20.20.70:FF:000364; Inosine-5'-monophosphate dehydrogenase 2; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
DR PROSITE; PS51917; PRU; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000479000}.
FT DOMAIN 121..182
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 187..245
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 385..493
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
SQ SEQUENCE 545 AA; 59994 MW; 7619DF04A8B28364 CRC64;
MPRFDSQINS MALQNGDTDE LVDGLTGSQL INNGDGLTYN DFILLPGFID FLPKDVELES
PLTKNITLQA PLVSSPMDTV TESDMAVAMA LCGGIGIIHR NCTVEYQANE VHKVKKYKHG
FIRDPVVLSP SHTVEDVFNV KKEHGFCGIP ITENGKLGGK LSGIVTSRDI DFIEDPKQRL
ASLDSVMTPL DKIVTARSDV DLKEANRILE RSKKGKLPII NEHGELVALI ARTDLKKSRN
YPNASKDENK QLLVGAAIGT TDGDKERIRA LAAAGVDVVV IDSSQGNSTY QIDMVKHIKA
NYPKLQVIGG NVVTTTQAKS LIDAGVDGLR VGMGSGSICI TQEVMAVGRA QGTAVYKKND
MTQETKKKGP TMTGGFPLWP RASPSRRNRL LEFKAGKMYM IGNMVYPDPR KGLDDFGTVH
LCWMDRITGT VEDDYHTEPM DCTYQRIEKC KTGRVYVLKM KKTKRTMFFW MQEPKMDRDA
FIAARVSHLV KSAVRVPLVY GIPMSLWDSC LSLADTSIAA NITQSILSFP GDQLARLSSS
NDRVS
//