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Database: UniProt
Entry: A0A6H5GQU0_9HEMI
LinkDB: A0A6H5GQU0_9HEMI
Original site: A0A6H5GQU0_9HEMI 
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
//
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