(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHG4_GEOS0

ID   A0A0F6BHG4_GEOS0        Unreviewed;       488 AA.
AC   A0A0F6BHG4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 25.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
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, ECO:0000256|RuleBase:RU003928};
GN   Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964};
GN   OrderedLocusNames=GY4MC1_0009 {ECO:0000313|EMBL:ADP72865.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72865.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72865.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72865.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU003928};
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       ECO:0000256|RuleBase:RU003928}.
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; CP002293; ADP72865.1; -; Genomic_DNA.
DR   RefSeq; WP_013399793.1; NC_014650.1.
DR   EnsemblBacteria; ADP72865; ADP72865; GY4MC1_0009.
DR   KEGG; gmc:GY4MC1_0009; -.
DR   KO; K00088; -.
DR   OMA; SSMGYCG; -.
DR   OrthoDB; 532857at2; -.
DR   BioCyc; GSP581103:G1GOQ-14-MONOMER; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000002034; Chromosome.
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; IPR015875; IMP_DH/GMP_Rdtase_CS.
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.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHG4.
DR   SWISS-2DPAGE; A0A0F6BHG4.
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003928};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003928};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-3,
KW   ECO:0000256|RuleBase:RU003928};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003927, ECO:0000313|EMBL:ADP72865.1};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003928}.
FT   DOMAIN       95    153       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   DOMAIN      157    215       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   NP_BIND     251    253       NAD. {ECO:0000256|PIRSR:PIRSR000130-3}.
FT   NP_BIND     301    303       NAD. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-3}.
FT   REGION      341    343       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   REGION      364    365       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   REGION      388    392       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   ACT_SITE    308    308       Thioimidate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-1}.
FT   ACT_SITE    404    404       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                1}.
FT   METAL       303    303       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       308    308       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       470    470       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       471    471       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       472    472       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   BINDING     251    251       NAD. {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   BINDING     306    306       IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-2}.
FT   BINDING     416    416       IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-2}.
SQ   SEQUENCE   488 AA;  53185 MW;  0AA398317C5E96CB CRC64;
     MWESKFAKEG LTFDDVLLIP AKSDVLPRDV DVTTKLSETL QLNIPIISAG MDTVTEAEMA
     IAMARQGGLG IIHKNMSIEQ QAEQVDKVKR SERGVITDPF FLTPEHQVYD AEHLMSKYRI
     SGVPIVNNEE EQKLVGIITN RDLRFIQDYS TKISDVMTKE NLITAPVGTT LEEAEKILQK
     YKVEKLPLVD ENGILKGLIT IKDIEKVIEF PNSAKDAKGR LLVGAAVGVT ADTMIRVKKL
     VEANVDVIVV DTAHGHSKGV LETVRKIREQ YPDLNIIAGN VATAEATRDL IEAGANIIKV
     GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGVPIIA DGGIKYSGDI VKALAAGAHA
     VMLGSLLAGV SESPGETEIY QGRRFKVYRG MGSVAAMEKG SKDRYFQEDN KKFVPEGIEG
     RVPYKGPLAD TIYQLVGGLR AGMGYCGTRN LEELREKTQF IRMTSAGLRE SHPHDVQITK
     EAPNYSIS
//

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