(data stored in ACNUC7421 zone)

SWISSPROT: Q3KIP9_PSEPF

ID   Q3KIP9_PSEPF            Unreviewed;       539 AA.
AC   Q3KIP9;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 113.
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=ATIC {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=IMP synthase {ECO:0000256|HAMAP-Rule:MF_00139};
GN   Name=purH {ECO:0000256|HAMAP-Rule:MF_00139};
GN   OrderedLocusNames=Pfl01_0613 {ECO:0000313|EMBL:ABA72357.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72357.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72357.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72357.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-
CC         beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-
CC         tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-
CC         4-carboxamide; Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57454, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475;
CC         EC=2.1.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00139,
CC         ECO:0000256|SAAS:SAAS01117956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-
CC         4-carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00139,
CC         ECO:0000256|SAAS:SAAS01117952};
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:SAAS00010681}.
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:SAAS00010501}.
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:SAAS00538992}.
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DR   EMBL; CP000094; ABA72357.1; -; Genomic_DNA.
DR   STRING; 205922.Pfl01_0613; -.
DR   World-2DPAGE; 0008:Q3KIP9; -.
DR   PRIDE; Q3KIP9; -.
DR   EnsemblBacteria; ABA72357; ABA72357; Pfl01_0613.
DR   KEGG; pfo:Pfl01_0613; -.
DR   eggNOG; ENOG4105DC1; Bacteria.
DR   eggNOG; COG0138; LUCA.
DR   HOGENOM; HOG000230373; -.
DR   KO; K00602; -.
DR   OMA; WRVAKFV; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
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_dup_dom_sf.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR002695; PurH-like.
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; Q3KIP9.
DR   SWISS-2DPAGE; Q3KIP9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00420855, ECO:0000313|EMBL:ABA72357.1};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00420897};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00420887};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00420854}.
FT   DOMAIN       26    139       MGS. {ECO:0000259|SMART:SM00851}.
SQ   SEQUENCE   539 AA;  57941 MW;  E1623315063C70CB CRC64;
     MEIEMTDQTT RLPIRRALIS VSDKTGILEF ARELEALGVE ILSTGGTFKL LQDNGVAAVE
     VADYTGFAEM MDGRVKTLHP KIHGGILGRR GIDDAIMNEH GIKPIDLVAV NLYPFEATIS
     KPGCDLPTAI ENIDIGGPTM VRSAAKNHKD VAIVVNASDY ADVLENLKAG GLTYAQRFDL
     MLKAFEHTAA YDGMIANYMG TVNQAAETLS TEGRSEFPRT FNSQFIKAQE MRYGENPHQS
     AAFYVEAKPA EVGIATATQL QGKELSYNNV ADTDAALECV KSFVKPACVI VKHANPCGVA
     VSPDAEGGIR QAYELAYATD TESAFGGIIA FNRELDAETA KAIVERQFVE VIIAPSVSEE
     ARAIVAAKAN VRLLACGEWS ADRVPAWDYK RVNGGLLVQS RDIGMIGADD LKVVTKRAPT
     EQEVHDLIFA WKVAKFVKSN AIVYAKNRQT IGVGAGQMSR VNSARIAAIK AEHAGLQVAG
     SVMASDAFFP FRDGLDNAAK VGITAVIQPG GSMRDAEVIA AADEAGIAMV FTGMRHFRH
//

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