(data stored in SCRATCH zone)

SWISSPROT: D3VJE2_XENNA

ID   D3VJE2_XENNA            Unreviewed;       529 AA.
AC   D3VJE2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
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   ECO:0000313|EMBL:CBJ88698.1};
GN   OrderedLocusNames=XNC1_0624 {ECO:0000313|EMBL:CBJ88698.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88698.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88698.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88698.1; -; Genomic_DNA.
DR   RefSeq; WP_013183370.1; NC_014228.1.
DR   STRING; 406817.XNC1_0624; -.
DR   EnsemblBacteria; CBJ88698; CBJ88698; XNC1_0624.
DR   KEGG; xne:XNC1_0624; -.
DR   eggNOG; ENOG4105DC1; Bacteria.
DR   eggNOG; COG0138; LUCA.
DR   HOGENOM; HOG000230372; -.
DR   KO; K00602; -.
DR   OMA; WRVAKFV; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000008075; 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; D3VJE2.
DR   SWISS-2DPAGE; D3VJE2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00420855, ECO:0000313|EMBL:CBJ88698.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00139,
KW   ECO:0000256|SAAS:SAAS00420854, ECO:0000313|EMBL:CBJ88698.1}.
FT   DOMAIN       19    132       MGS. {ECO:0000259|SMART:SM00851}.
SQ   SEQUENCE   529 AA;  57339 MW;  CDC20C4FB70E2F7E CRC64;
     MQQLRPIRRA LLSVSDKAGV VEFAKALSSR GVKLLSTGGT AHLLSEAGLN VTEVSDHTGF
     PEMMDGRVKT LHPKIHGGIL GRRGLDDEVM VQHQIAPIDM VVVNLYPFAQ TVAKPDCSLE
     DAIENIDIGG PTMVRSAAKN HKDVTIVVNS QDYNKIIEEM DSHQNSLTHA TRFDLAIKAF
     EHTTAYDSMI ANYFGKLVAP YHGETDQPSG RFPRTLNLNL IKKQDMRYGE NSHQDAAFYI
     EEQIAEASIA TAAQLQGKAL SYNNIADTDA ALECVKAFSE PACVIVKHAN PCGVAVSTDI
     HTAYDQAFKT DPTSAFGGII AFNRALDADT AKSIIERQFV EVIIAPSINE TALPILATKQ
     NVRVLACGEW RSPVAGLDFK RVNGGLLVQD RDLGMVTEDD LRVVSKRQPT KQEMQDALFC
     WKVAKFVKSN AIVYAKDNMT VGIGAGQMSR VYSAKIAGIK AADEGLDVQG CAMASDAFFP
     FRDGIDAAAA VGVSCVIQPG GSIRDDEVIA AADEQGIAMI FTGMRHFRH
//

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