(data stored in SCRATCH zone)

SWISSPROT: D1CER5_THET1

ID   D1CER5_THET1            Unreviewed;       490 AA.
AC   D1CER5;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964};
DE            Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964};
DE            Short=IMPD {ECO:0000256|HAMAP-Rule:MF_01964};
DE            Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_01964};
DE            EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_01964};
GN   Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964};
GN   OrderedLocusNames=Tter_0500 {ECO:0000313|EMBL:ACZ41421.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41421.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41421.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP)
CC       to xanthosine 5'-phosphate (XMP), the first committed and rate-
CC       limiting step in the de novo synthesis of guanine nucleotides, and
CC       therefore plays an important role in the regulation of cell
CC       growth. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP;
CC         Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01964};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01964};
CC   -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive
CC       inhibitor that prevents formation of the closed enzyme
CC       conformation by binding to the same site as the amobile flap. In
CC       contrast, mizoribine monophosphate (MZP) is a competitive
CC       inhibitor that induces the closed conformation. MPA is a potent
CC       inhibitor of mammalian IMPDHs but a poor inhibitor of the
CC       bacterial enzymes. MZP is a more potent inhibitor of bacterial
CC       IMPDH. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
CC       XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP-
CC       Rule:MF_01964, ECO:0000256|RuleBase:RU003927}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}.
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DR   EMBL; CP001825; ACZ41421.1; -; Genomic_DNA.
DR   RefSeq; WP_012874456.1; NC_013525.1.
DR   STRING; 525904.Tter_0500; -.
DR   EnsemblBacteria; ACZ41421; ACZ41421; Tter_0500.
DR   KEGG; ttr:Tter_0500; -.
DR   eggNOG; ENOG4105CP4; Bacteria.
DR   eggNOG; COG0516; LUCA.
DR   eggNOG; COG0517; LUCA.
DR   HOGENOM; HOG000165754; -.
DR   KO; K00088; -.
DR   OMA; SSMGYCG; -.
DR   OrthoDB; 532857at2; -.
DR   BioCyc; TTER525904:G1GGS-504-MONOMER; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000000323; Chromosome 1.
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; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01964; IMPDH; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 1.
DR   SMART; SM00116; CBS; 2.
DR   TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   3: Inferred from homology;
DR   PRODOM; D1CER5.
DR   SWISS-2DPAGE; D1CER5.
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01964};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-
KW   3};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003927, ECO:0000313|EMBL:ACZ41421.1};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|PIRSR:PIRSR000130-4};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   DOMAIN       95    153       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   DOMAIN      155    212       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   NP_BIND     249    251       NAD. {ECO:0000256|PIRSR:PIRSR000130-3}.
FT   NP_BIND     298    300       NAD. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-3}.
FT   REGION      338    340       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964}.
FT   REGION      361    362       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964}.
FT   REGION      385    389       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964}.
FT   ACT_SITE    305    305       Thioimidate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-1}.
FT   ACT_SITE    403    403       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                1}.
FT   METAL       300    300       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       302    302       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       305    305       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       472    472       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       473    473       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       474    474       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   BINDING     249    249       NAD. {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   BINDING     418    418       IMP. {ECO:0000256|HAMAP-Rule:MF_01964}.
SQ   SEQUENCE   490 AA;  52485 MW;  59B0DC6E930912AF CRC64;
     MLDDKFALEG YTFDDVLLVP AYSEVLPSEV STSTCLTPRI SLNIPIVSAA MDTVTEARMA
     IALAREGGIG IIHRNLSIEE QVAEVDKVKR SEAGMIVEPV TLPPYAQLSD AVAIMEKYHI
     SGVPVVDEEG KLVGILTNRD IRFETDLTKP ISSAMTSENL ITAPVGTTLE EAREILHRYK
     IEKLPVVDDE GRLKGLITVK DIQKKIQFPM ATKDEKGRLR VGAAVGVGPA GLERAEALIA
     AGVDVIVVDT AHGHTKAVID IVREIKARWD VDVIAGNVGT PEGAEDLVRA GADGVKVGIG
     PGAICTTRIV AGAGVPQLTA IYNCARAVAP YGATIIADGG IQYSGDIAKA IAAGADTVML
     GSLLAGVDES PGEVLIYQGE RYKEYRGMGS IAAMKQRGYS RDRYGQADIG NVSKLVPEGI
     EARVPYKGPL SNLVYQLVGG LRSAMGYCGA RNIREMKENT KFMRITNAGL RESHPHDVVI
     TREAPNYRLR
//

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