PUR9_SALTY
ID PUR9_SALTY Reviewed; 529 AA.
AC P26978; Q9L9H7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
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}; OrderedLocusNames=STM4176;
GN ORFNames=STMF1.30;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-529.
RX PubMed=1954258; DOI=10.1016/0167-4781(91)90202-w;
RA Chopra A.K., Peterson J.W., Prasad R.;
RT "Nucleotide sequence analysis of purH and purD genes from Salmonella
RT typhimurium.";
RL Biochim. Biophys. Acta 1090:351-354(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; EC=2.1.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 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, ECO:0000305}.
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DR EMBL; AF170176; AAF33520.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23004.1; -; Genomic_DNA.
DR EMBL; M66160; AAA27197.1; -; Genomic_DNA.
DR PIR; S18488; DTEBPH.
DR RefSeq; NP_463045.1; NC_003197.2.
DR RefSeq; WP_001187509.1; NC_003197.2.
DR AlphaFoldDB; P26978; -.
DR SMR; P26978; -.
DR STRING; 99287.STM4176; -.
DR PaxDb; P26978; -.
DR EnsemblBacteria; AAL23004; AAL23004; STM4176.
DR GeneID; 1255702; -.
DR KEGG; stm:STM4176; -.
DR PATRIC; fig|99287.12.peg.4390; -.
DR HOGENOM; CLU_016316_5_2_6; -.
DR OMA; WRVAKFV; -.
DR PhylomeDB; P26978; -.
DR BioCyc; SENT99287:STM4176-MON; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
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.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..529
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_0000192120"
FT DOMAIN 1..148
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT CONFLICT 302..303
FT /note="DA -> EP (in Ref. 2; AAA27197)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="A -> R (in Ref. 2; AAA27197)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="L -> W (in Ref. 2; AAA27197)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="S -> T (in Ref. 2; AAA27197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 57467 MW; 5D713504AD644778 CRC64;
MQQRRPVRRA LLSVSDKAGI IEFAQALSAR GVELLSTGGT ARLLAEKGLP VTEVSDYTGF
PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EQHHIAPIDM VVVNLYPFAE TVAREGCSLE
DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYDAIIKEM DANEGSLTLD TRFDLAIKAF
EHTAAYDSMI ANYFGSMVPA YHGESKEAAG RFPRTLNLNF IKKQDMRYGE NSHQQAAFYI
EENVKEASVA TAQQVQGKAL SYNNIADTDA ALECVKEFNE PACVIVKHAN PCGVAVSTTI
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSATE EALKITAAKQ
NVRVLTCGQW AQRVPGLDFK RVNGGLLVQD RDLGMVSEAE LRVVSKRQPT EQELRDALFC
WKVAKFVKSN AIVYAKENMT IGIGAGQMSR VYSAKIAGIK AADEGLEVKG SAMASDAFFP
FRDGIDAAAA VGVSCVIQPG GSIRDDEVIA AADEHGIAMI FTDMRHFRH
