(data stored in SCRATCH zone)

SWISSPROT: C3MGQ8_SINFN

ID   C3MGQ8_SINFN            Unreviewed;       514 AA.
AC   C3MGQ8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 63.
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=NGR_c03770 {ECO:0000313|EMBL:ACP24173.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24173.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24173.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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: Inosine 5'-phosphate + NAD(+) + H(2)O =
CC       xanthosine 5'-phosphate + NADH. {ECO:0000256|HAMAP-Rule:MF_01964,
CC       ECO:0000256|RuleBase:RU003928}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01964};
CC   -!- ENZYME 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; CP001389; ACP24173.1; -; Genomic_DNA.
DR   RefSeq; WP_012706958.1; NC_012587.1.
DR   RefSeq; YP_002824926.1; NC_012587.1.
DR   ProteinModelPortal; C3MGQ8; -.
DR   STRING; 394.NGR_c03770; -.
DR   EnsemblBacteria; ACP24173; ACP24173; NGR_c03770.
DR   GeneID; 7791603; -.
DR   KEGG; rhi:NGR_c03770; -.
DR   PATRIC; fig|394.7.peg.3182; -.
DR   eggNOG; ENOG4105CP4; Bacteria.
DR   eggNOG; COG0516; LUCA.
DR   HOGENOM; HOG000165755; -.
DR   KO; K00088; -.
DR   OMA; GIGIVHK; -.
DR   OrthoDB; POG091H02IM; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP.
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; C3MGQ8.
DR   SWISS-2DPAGE; C3MGQ8.
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN      112    175       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   DOMAIN      179    236       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   NP_BIND     273    275       NAD. {ECO:0000256|PIRSR:PIRSR000130-3}.
FT   NP_BIND     323    325       NAD. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-3}.
FT   REGION      363    365       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   REGION      386    387       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   REGION      410    414       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   ACT_SITE    330    330       Thioimidate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-1}.
FT   ACT_SITE    426    426       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                1}.
FT   METAL       325    325       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       327    327       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       330    330       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       495    495       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       496    496       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       497    497       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   BINDING     273    273       NAD. {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   BINDING     328    328       IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-2}.
FT   BINDING     441    441       IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-2}.
SQ   SEQUENCE   514 AA;  53749 MW;  79DB65C14A3DA39B CRC64;
     MVPGDFRIFE EELAMARIIE TATGLEALTF DDVLLQPGHS EVMPGQTNIA TRIAQDIDLN
     LPILSAAMDT VTEARLAIAM AQAGGIGVIH RNLTPAEQAE EVRQVKKFES GMVVNPVTIG
     PDATLADALS LMKAHGISGI PVVENGGSGG QTQGRLVGIL TNRDVRFASD PSQKIYELMT
     RENLVTVKES VDQQEAKRLL HKHRIEKLLV VDPDGRCVGL ITVKDIEKSQ LNPNASKDSQ
     GRLRAAAAVS VGDDGLERAE RLIDAGVDLI VVDTAHGHSQ RVLDAVARVK KMSNSVRIMA
     GNVATADGTK ALMDAGADAV KVGIGPGSIC TTRIVAGVGV PQLAAIMAAV EAAQASGIPV
     IADGGIKYSG DLAKAIAAGA SAVMVGSLLA GTEESPGEVF LYQGRSFKAY RGMGSVGAMA
     RGSADRYFQA EVRDTLKLVP EGIEGQVPYK GPVGGVLHQL AGGLKASMGY VGGATIKDYQ
     QRATFVRISG AGLRESHAHD VTITRESPNY PGGA
//

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