(data stored in ACNUC7421 zone)

SWISSPROT: PUR9_SHESH

ID   PUR9_SHESH              Reviewed;         534 AA.
AC   A8FQD4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000255|HAMAP-Rule:MF_00139};
DE   Includes:
DE     RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_00139};
DE              EC=2.1.2.3 {ECO:0000255|HAMAP-Rule:MF_00139};
DE     AltName: Full=AICAR transformylase {ECO:0000255|HAMAP-Rule:MF_00139};
DE   Includes:
DE     RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00139};
DE              EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00139};
DE     AltName: Full=ATIC {ECO:0000255|HAMAP-Rule:MF_00139};
DE     AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00139};
DE     AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00139};
GN   Name=purH {ECO:0000255|HAMAP-Rule:MF_00139};
GN   OrderedLocusNames=Ssed_0444;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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:0000255|HAMAP-Rule:MF_00139}.
CC   -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamide. {ECO:0000255|HAMAP-
CC       Rule:MF_00139}.
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:0000255|HAMAP-Rule:MF_00139}.
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:0000255|HAMAP-Rule:MF_00139}.
CC   -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC       region. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC   -!- SIMILARITY: Belongs to the PurH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00139}.
DR   EMBL; CP000821; ABV35057.1; -; Genomic_DNA.
DR   RefSeq; WP_012140794.1; NC_009831.1.
DR   ProteinModelPortal; A8FQD4; -.
DR   SMR; A8FQD4; -.
DR   STRING; 425104.Ssed_0444; -.
DR   PRIDE; A8FQD4; -.
DR   EnsemblBacteria; ABV35057; ABV35057; Ssed_0444.
DR   KEGG; sse:Ssed_0444; -.
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   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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; A8FQD4.
DR   SWISS-2DPAGE; A8FQD4.
KW   Complete proteome; Hydrolase; Multifunctional enzyme;
KW   Purine biosynthesis; Transferase.
FT   CHAIN         1    534       Bifunctional purine biosynthesis protein
FT                                PurH.
FT                                /FTId=PRO_1000076495.
SQ   SEQUENCE   534 AA;  57499 MW;  F31C3217A554A2F3 CRC64;
     MNNARPIRRA LLSVSDKTGI LEFAKSLHAQ GVELLSTGGT ARLLADNGVP VIEVSDHTGH
     PEIMDGRVKT LHPKVHGGIL ARRGIDELVM EQNNIKPIDL VAVNLYPFAE TVAKEGCTLA
     DAVENIDIGG PTMVRSTAKN HKDTTIIVNA SDYDRVIVEM NANEGSTTLE TRFDLAIAAF
     EHTAAYDGMI ANYFGTQVPA HSKDECHHDS KFPRTYNTQL VKKQDLRYGE NSHQTAAFYV
     DSPSFNGQGD EASVASAIQL QGKALSYNNI ADTDSALECV KEFSEPACVI VKHANPCGVA
     IGSDLLDAYN RAFKTDPTSA FGGIIAFNGE LDAATASAIV ERQFVEVIIA PKVSQAARDI
     VAAKANLRLL ECGEWNTKTT SLDYKRVNGG LLLQDRDQGM VGLDDVKVVS KRQPTAAEMK
     DLMFCWKVAK FVKSNAIVYA KDSMTIGVGA GQMSRVYSAK VAGIKAADEG LEVQDSVMAS
     DAFFPFRDGI DAAAAAGISC IIQPGGSIRD EEIIAAADEH GMAMVFTGMR HFRH
//

If you have problems or comments...

PBIL Back to PBIL home page