(data stored in SCRATCH zone)

SWISSPROT: D4YXQ2_SPHJU

ID   D4YXQ2_SPHJU            Unreviewed;       529 AA.
AC   D4YXQ2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 52.
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   ECO:0000313|EMBL:BAI95134.1};
GN   OrderedLocusNames=SJA_C1-03000 {ECO:0000313|EMBL:BAI95134.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95134.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95134.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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; AP010803; BAI95134.1; -; Genomic_DNA.
DR   RefSeq; WP_013038926.1; NC_014006.1.
DR   ProteinModelPortal; D4YXQ2; -.
DR   STRING; 452662.SJA_C1-03000; -.
DR   EnsemblBacteria; BAI95134; BAI95134; SJA_C1-03000.
DR   GeneID; 29272003; -.
DR   KEGG; sjp:SJA_C1-03000; -.
DR   eggNOG; ENOG4105DC1; Bacteria.
DR   eggNOG; COG0138; LUCA.
DR   HOGENOM; HOG000230372; -.
DR   KO; K00602; -.
DR   OMA; DLLFAWK; -.
DR   OrthoDB; POG091H00UT; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000007753; Chromosome 1.
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; D4YXQ2.
DR   SWISS-2DPAGE; D4YXQ2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00632544, ECO:0000313|EMBL:BAI95134.1};
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:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00632542, ECO:0000313|EMBL:BAI95134.1}.
FT   DOMAIN       18    132       MGS. {ECO:0000259|SMART:SM00851}.
SQ   SEQUENCE   529 AA;  55400 MW;  5F37B5FF4CCCF067 CRC64;
     MSDVTIKRAL LSVSDKSGLI ELGQALGRHG VELVSTGGTA KALREAGLAV KDISDLTGFP
     EMMDGRVKTL HPKVHGGLLA VRGNAEHVAA MQAHDIGAID LVVVNLYPFA ATVAKGADRE
     EIIENIDIGG PSMVRSAAKN HESVAIVTDP ADYARLVAEM EEKGGATSYD FRRMLAAKAY
     AATAAYDSMI ASWFAFADQG AQFPESLSVS SRLGSTLRYG ENPHQSAALY LPVGPSANGI
     AQARQVQGKE LSYNNYNDAD AALELVSEFR DGPPTVVIVK HANPCGVATG ATLIEAYEAA
     LACDSVSAFG GIIAVNRPLD GPTAEAISGI FTEVVAAPDA DEDAKAIFAK KKNLRLLLTG
     DLPDPARPGL QIKSIAGGLL VQGRDNGRIT RDQLKVVTKR APTEQELNDC LFAWTVAKHV
     KSNAIVYAKA GSTAGIGAGQ MNRLESARIA AWKAKDAAEK AGWAEARTLG SAVASDAFFP
     FADGLLAAVE AGATAVIQPG GSIRDEEVIA AADEAGLAMV FTGMRHFRH
//

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