(data stored in ACNUC7421 zone)

SWISSPROT: IMDH_BACSU

ID   IMDH_BACSU              Reviewed;         488 AA.
AC   P21879;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   11-DEC-2019, entry version 156.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMPD {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_01964};
DE            EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_01964};
DE   AltName: Full=Superoxide-inducible protein 12;
DE            Short=SOI12;
GN   Name=guaB {ECO:0000255|HAMAP-Rule:MF_01964}; Synonyms=gnaB;
GN   OrderedLocusNames=BSU00090;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1979163; DOI=10.1093/nar/18.22.6710;
RA   Kanzaki N., Miyagawa K.I.;
RT   "Nucleotide sequence of the Bacillus subtilis IMP dehydrogenase gene.";
RL   Nucleic Acids Res. 18:6710-6710(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-25.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
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:0000255|HAMAP-Rule:MF_01964}.
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:0000255|HAMAP-Rule:MF_01964};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01964};
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:0000255|HAMAP-Rule:MF_01964}.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC       from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964}.
CC   -!- INDUCTION: By superoxide.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
CC       Rule:MF_01964}.
DR   EMBL; X55669; CAA39204.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05245.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11785.1; -; Genomic_DNA.
DR   PIR; S66039; DEBSMP.
DR   RefSeq; NP_387890.1; NC_000964.3.
DR   RefSeq; WP_003226803.1; NZ_JNCM01000024.1.
DR   SMR; P21879; -.
DR   IntAct; P21879; 1.
DR   MINT; P21879; -.
DR   STRING; 224308.BSU00090; -.
DR   jPOST; P21879; -.
DR   PaxDb; P21879; -.
DR   PRIDE; P21879; -.
DR   EnsemblBacteria; CAB11785; CAB11785; BSU00090.
DR   GeneID; 938032; -.
DR   KEGG; bsu:BSU00090; -.
DR   PATRIC; fig|224308.179.peg.9; -.
DR   eggNOG; ENOG4105CP4; Bacteria.
DR   eggNOG; COG0516; LUCA.
DR   eggNOG; COG0517; LUCA.
DR   HOGENOM; HOG000165754; -.
DR   InParanoid; P21879; -.
DR   KO; K00088; -.
DR   OMA; SSMGYCG; -.
DR   PhylomeDB; P21879; -.
DR   BioCyc; BSUB:BSU00090-MONOMER; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IBA:GO_Central.
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   GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
DR   PRODOM; P21879.
DR   SWISS-2DPAGE; P21879.
KW   CBS domain; Direct protein sequencing; GMP biosynthesis; Metal-binding;
KW   NAD; Oxidoreductase; Potassium; Purine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN           1..488
FT                   /note="Inosine-5'-monophosphate dehydrogenase"
FT                   /id="PRO_0000093691"
FT   DOMAIN          95..153
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   DOMAIN          157..214
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   NP_BIND         301..303
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   REGION          341..343
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   REGION          364..365
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   REGION          388..392
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   ACT_SITE        308
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   ACT_SITE        404
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           303
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           305
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           308
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           470
FT                   /note="Potassium; via carbonyl oxygen; shared with
FT                   tetrameric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           471
FT                   /note="Potassium; via carbonyl oxygen; shared with
FT                   tetrameric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           472
FT                   /note="Potassium; via carbonyl oxygen; shared with
FT                   tetrameric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         251
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         306
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         416
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   CONFLICT        28
FT                   /note="R -> H (in Ref. 1; CAA39204)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        480..488
FT                   /note="KESPNYTIS -> VHRNKALPGLFGSHQKKTGFVYDECCQSGFFSSD (in
FT                   Ref. 1; CAA39204)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   488 AA;  52991 MW;  34939E2758EA48B6 CRC64;
     MWESKFSKEG LTFDDVLLVP AKSEVLPRDV DLSVELTKTL KLNIPVISAG MDTVTESAMA
     IAMARQGGLG IIHKNMSIEQ QAEQVDKVKR SERGVITNPF FLTPDHQVFD AEHLMGKYRI
     SGVPIVNNEE DQKLVGIITN RDLRFISDYS MKISDVMTKE ELVTASVGTT LDEAEKILQK
     HKIEKLPLVD DQNKLKGLIT IKDIEKVIEF PNSSKDIHGR LIVGAAVGVT GDTMTRVKKL
     VEANVDVIVI DTAHGHSQGV LNTVTKIRET YPELNIIAGN VATAEATRAL IEAGADVVKV
     GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGKTIIA DGGIKFSGDI TKALAAGGHA
     VMLGSLLAGT SESPGETEIY QGRRFKVYRG MGSVAAMEKG SKDRYFQEEN KKFVPEGIEG
     RTPYKGPVEE TVYQLVGGLR SGMGYCGSKD LRALREEAQF IRMTGAGLRE SHPHDVQITK
     ESPNYTIS
//

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