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Database: UniProt
Entry: Q4S7W7_TETNG
LinkDB: Q4S7W7_TETNG
Original site: Q4S7W7_TETNG 
ID   Q4S7W7_TETNG            Unreviewed;       539 AA.
AC   Q4S7W7;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=IMP dehydrogenase {ECO:0000256|ARBA:ARBA00024384};
DE            EC=1.1.1.205 {ECO:0000256|ARBA:ARBA00024384};
DE   Flags: Fragment;
GN   ORFNames=GSTENG00022603001 {ECO:0000313|EMBL:CAG03265.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG03265.1};
RN   [1] {ECO:0000313|EMBL:CAG03265.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|EMBL:CAG03265.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; 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:ARBA00024264};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC       from IMP: step 1/1. {ECO:0000256|ARBA:ARBA00024330}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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:CAG03265.1}.
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DR   EMBL; CAAE01014710; CAG03265.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4S7W7; -.
DR   KEGG; tng:GSTEN00022603G001; -.
DR   UniPathway; UPA00601; UER00295.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd04601; CBS_pair_IMPDH; 1.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01964; IMPDH; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   PANTHER; PTHR11911:SF121; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE 2; 1.
DR   PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00478; IMPDH; 2.
DR   PIRSF; PIRSF000130; IMPDH; 2.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM01240; IMPDH; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 2.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|PIRSR:PIRSR000130-3};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4}.
FT   DOMAIN          115..174
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          180..238
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        332
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT   ACT_SITE        454
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT   BINDING         275..277
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         325..327
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         327
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         329
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         332
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT   NON_TER         539
FT                   /evidence="ECO:0000313|EMBL:CAG03265.1"
SQ   SEQUENCE   539 AA;  58317 MW;  5863AB64F2D58777 CRC64;
     SMADYLISGQ TGYVPEDGLA GQQLFGCGDG LTYNDFLILP GYINFTSDQV DLTSALTKKI
     TMKTPFVSSP MDTVTEANMA IAMALTGGIG FIHHNCTPEF QANEVRKVKR YEQGFITDPV
     VMSPNERVRD VFQAKARHGF CGIPITDNGK MGGKLVGIIS SRDIDFLKEE DHDLPLNEVM
     TKREDLVVAP AGVTLKEANE ILQRSKKGKL PIVNEQGSLV SIIARTDLKK NRDFPLASKD
     SRKQLLCGAA IGTHNDDKYR LDLLVQSGVD VVVLDSSQGN SIFQINMIKY IKEKYPTLQV
     IGGNVVTAAQ AKNLIDAGVD ALRVGMGSGS ICITQEASLS IPPAIKLHSP KTHTTVTGYS
     MLACGRPQAT AVYKVSEYAR RFGVPVIADG GIQNVGHVAK ALALGACTVM MGSLLAATSE
     APGEYFFSDG IRLKKYRGMG SLDAMDKNLG SQTRYFSESD KIKVAQGVSG AVQDKGSIHK
     FVPYLLAGIQ HSCQDIGAKS LTQLRAMMYS GDLKFERRTA SAQIEGGVHS LHSYEKRLF
//
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