(data stored in ACNUC7421 zone)

SWISSPROT: C5BHF4_EDWI9

ID   C5BHF4_EDWI9            Unreviewed;       529 AA.
AC   C5BHF4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 62.
DE   RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000256|HAMAP-Rule:MF_00139};
DE   Includes:
DE     RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_00139};
DE              EC=2.1.2.3 {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=AICAR transformylase {ECO:0000256|HAMAP-Rule:MF_00139};
DE   Includes:
DE     RecName: Full=IMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_00139};
DE              EC=3.5.4.10 {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=Inosinicase {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=IMP synthase {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=ATIC {ECO:0000256|HAMAP-Rule:MF_00139};
GN   Name=purH {ECO:0000256|HAMAP-Rule:MF_00139};
GN   OrderedLocusNames=NT01EI_0186 {ECO:0000313|EMBL:ACR67432.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67432.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
CC       {ECO:0000256|HAMAP-Rule:MF_00139, ECO:0000256|SAAS:SAAS00632554}.
CC   -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamide. {ECO:0000256|HAMAP-Rule:MF_00139,
CC       ECO:0000256|SAAS:SAAS00632535}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl
CC       THF route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00139,
CC       ECO:0000256|SAAS:SAAS00632546}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC       carboxamide: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00139,
CC       ECO:0000256|SAAS:SAAS00632543}.
CC   -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC       region. {ECO:0000256|HAMAP-Rule:MF_00139}.
CC   -!- SIMILARITY: Belongs to the PurH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00139, ECO:0000256|SAAS:SAAS00632536}.
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DR   EMBL; CP001600; ACR67432.1; -; Genomic_DNA.
DR   RefSeq; WP_015869644.1; NC_012779.2.
DR   ProteinModelPortal; C5BHF4; -.
DR   STRING; 634503.NT01EI_0186; -.
DR   EnsemblBacteria; ACR67432; ACR67432; NT01EI_0186.
DR   GeneID; 7958777; -.
DR   KEGG; eic:NT01EI_0186; -.
DR   PATRIC; fig|634503.3.peg.168; -.
DR   eggNOG; ENOG4105DC1; Bacteria.
DR   eggNOG; COG0138; LUCA.
DR   HOGENOM; HOG000230373; -.
DR   KO; K00602; -.
DR   OMA; DLLFAWK; -.
DR   OrthoDB; POG091H00UT; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.140.20; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   HAMAP; MF_00139; PurH; 1.
DR   InterPro; IPR024051; AICAR_Tfase_dom.
DR   InterPro; IPR002695; AICARFT_IMPCHas.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR011607; MGS-like_dom.
DR   PANTHER; PTHR11692; PTHR11692; 1.
DR   Pfam; PF01808; AICARFT_IMPCHas; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR   SMART; SM00798; AICARFT_IMPCHas; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR00355; purH; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHF4.
DR   SWISS-2DPAGE; C5BHF4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00632544, ECO:0000313|EMBL:ACR67432.1};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00632570};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00632540};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00632542, ECO:0000313|EMBL:ACR67432.1}.
FT   DOMAIN       19    132       MGS. {ECO:0000259|SMART:SM00851}.
SQ   SEQUENCE   529 AA;  57588 MW;  70F22FAE09E785CD CRC64;
     MQHSRPVRRA LLSVSDKSGI VEFAQALHLR GVELLSTGGT ARLLSQAGLP VTEVSDYTGF
     PEMMDGRVKT LHPKVHGGIL GRRDRDAAVM QQHGIQPIDM VVVNLYPFAQ TVARPDCSQE
     DAVENIDIGG PTMVRSAAKN HNDVAIVVNN GDFENIIAEM DAHHGALTQA TRFDLAIKAF
     EHTAAYDSMI ANYFGSLVAP YHGDIHSPSG RFPRTLNLNL VKKQDMRYGE NGHQQAAFYI
     EEPQVEACIA TAQQLQGKAL SYNNIADTDA ALECVKSFTE PACVIVKHAN PCGVALGDDL
     FDAYERAYQT DPTSAFGGII AFNRTLDAKT AQAIITRQFV EVIIAPHVTE DALDLLSAKQ
     NVRVLACDEW DVRVPGLDFK RVNGGLLVQD RDLDMVDAAD LRVVTERQPS EQELRDALFC
     WKVAKFVKSN AIVYARDNMT VGIGAGQMSR VYSAKIAGIK AADEGLQIAG SVMASDAFFP
     FRDGIDAAAA VGIRCVIQPG GSIRDDEVIA AANEHDIAMI FTGMRHFRH
//

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