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PURO_METJA
ID   PURO_METJA              Reviewed;         202 AA.
AC   Q58043;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   09-SEP-2003, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=IMP cyclohydrolase;
DE            EC=3.5.4.10;
DE   AltName: Full=IMP synthase;
DE   AltName: Full=Inosinicase;
GN   Name=purO; OrderedLocusNames=MJ0626;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=11844782; DOI=10.1128/jb.184.5.1471-1473.2002;
RA   Graupner M., Xu H., White R.H.;
RT   "New class of IMP cyclohydrolases in Methanococcus jannaschii.";
RL   J. Bacteriol. 184:1471-1473(2002).
CC   -!- FUNCTION: Catalyzes the cyclization of 5-formylamidoimidazole-4-
CC       carboxamide ribonucleotide to IMP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC         carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6-8.5.;
CC       Temperature dependence:
CC         Fully active at 80 degrees Celsius. Gradually loses some activity
CC         from 90 to 100 degrees Celsius.;
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC       from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC       1/1.
CC   -!- SIMILARITY: Belongs to the archaeal IMP cyclohydrolase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB98620.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB98620.1; ALT_INIT; Genomic_DNA.
DR   PIR; B64378; B64378.
DR   RefSeq; WP_064496562.1; NC_000909.1.
DR   AlphaFoldDB; Q58043; -.
DR   SMR; Q58043; -.
DR   STRING; 243232.MJ_0626; -.
DR   EnsemblBacteria; AAB98620; AAB98620; MJ_0626.
DR   GeneID; 1451492; -.
DR   KEGG; mja:MJ_0626; -.
DR   eggNOG; arCOG04727; Archaea.
DR   HOGENOM; CLU_1352116_0_0_2; -.
DR   InParanoid; Q58043; -.
DR   OMA; HVDPIAE; -.
DR   OrthoDB; 106750at2157; -.
DR   PhylomeDB; Q58043; -.
DR   BioCyc; MetaCyc:MON-14617; -.
DR   BRENDA; 3.5.4.10; 3260.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.20.20; -; 1.
DR   HAMAP; MF_00705; IMP_cyclohydrol; 1.
DR   InterPro; IPR010191; IMP_cyclohydrolase.
DR   InterPro; IPR020600; IMP_cyclohydrolase-like.
DR   InterPro; IPR036795; IMP_cyclohydrolase-like_sf.
DR   Pfam; PF07826; IMP_cyclohyd; 1.
DR   PIRSF; PIRSF004866; IMP_cclhdr_arch; 1.
DR   SUPFAM; SSF75569; SSF75569; 1.
DR   TIGRFAMs; TIGR01922; purO_arch; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..202
FT                   /note="IMP cyclohydrolase"
FT                   /id="PRO_0000145795"
SQ   SEQUENCE   202 AA;  22941 MW;  339DDF505D0733D9 CRC64;
     MYIGRFLVVG KTKEGKPFAA YRVSSRSFPN REAKKMDDNT VAIIPKDLNE MFKNPYITYN
     CIKVIDKTIV VSNGTHTDFI AEKLHFGKRD ALAYVLAVMD YEKDDYKTPR IAAILDENEC
     YMGYVAHDDI RVKKVELKDG KGYYLGVYNA CKIDENQIID IKGETAEEIA DYILNYEEFE
     HPVACAVAVI DKDGIKIATK GK
 
 
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