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Database: UniProt
Entry: A0A024GJS6_9STRA
LinkDB: A0A024GJS6_9STRA
Original site: A0A024GJS6_9STRA 
ID   A0A024GJS6_9STRA        Unreviewed;       502 AA.
AC   A0A024GJS6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
DE            Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156};
DE            Short=IMPD {ECO:0000256|HAMAP-Rule:MF_03156};
DE            Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_03156};
DE            EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
GN   ORFNames=BN9_079130 {ECO:0000313|EMBL:CCI46958.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI46958.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI46958.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI46958.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to
CC       xanthosine 5'-phosphate (XMP), the first committed and rate-limiting
CC       step in the de novo synthesis of guanine nucleotides, and therefore
CC       plays an important role in the regulation of cell growth.
CC       {ECO:0000256|HAMAP-Rule:MF_03156}.
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         ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958,
CC         ECO:0000256|HAMAP-Rule:MF_03156};
CC   -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive
CC       inhibitor that prevents formation of the closed enzyme conformation by
CC       binding to the same site as the amobile flap. In contrast, mizoribine
CC       monophosphate (MZP) is a competitive inhibitor that induces the closed
CC       conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor
CC       inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of
CC       bacterial IMPDH. {ECO:0000256|HAMAP-Rule:MF_03156}.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC       from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_03156,
CC       ECO:0000256|RuleBase:RU003928}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03156}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC       {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_03156,
CC       ECO:0000256|RuleBase:RU003927}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03156}.
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:CCI46958.1}.
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DR   EMBL; CAIX01000145; CCI46958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GJS6; -.
DR   STRING; 65357.A0A024GJS6; -.
DR   InParanoid; A0A024GJS6; -.
DR   OrthoDB; 166969at2759; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   NCBIfam; TIGR01302; IMP_dehydrog; 1.
DR   PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 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; 1.
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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW   Rule:MF_03156};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03156};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03156};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03156,
KW   ECO:0000256|RuleBase:RU003927};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03156};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_03156}; Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT   DOMAIN          171..227
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        321
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-1"
FT   ACT_SITE        417
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-1"
FT   BINDING         264..266
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         314..316
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         316
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|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         318
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|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         319
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT   BINDING         321
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|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         354..356
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT   BINDING         377..378
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT   BINDING         401..405
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT   BINDING         429
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
SQ   SEQUENCE   502 AA;  54272 MW;  F0E83D62B130A978 CRC64;
     MTDAFEDGES AANLFGKKNA GVAYTYDDLI LLPGHINFGV DSVRLESKIT KNISLHLPLI
     SSPMDTVTEH NMAIGMALHG GIGIIHYNMS IEEQCKEVRL VKKFENGFIT HPQCLSPTNS
     LADVDRIKSE FGFAGIPITE SGKIGSVLVG IVSNRDIDFI EDRTTLLSEV MTTDLVTAAE
     GISLVEANKI LKDSKKGKLP IVNAKGELVS LISRRDLLKN REFPHASKDS NKQLLVGAAI
     GTRLHDRERC SALVDAGVNL IVIDSSQGDS IFQIELIQWI KSTHPTVDVI GGNVVTRRQA
     HSLIEAGADG LKIGMGVGSI CTTQEVCAVG RAQASAVYET ATYARKFNVP VIADGGIGSC
     GHIIKALSLG AAAVMCGSLF AGTEEAPGQY YFQDGVRLKK YRGMGSVEAM VQGSSKRYFA
     HSASVKVAQG VTGAVVDKGT LKEYLPYLQQ GIRHGLQDLG YDSIIKLHAA LHQEQLRFEL
     RTPAAQREGN VHSLYSYEKR LY
//
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