PURU_SHIFL
ID PURU_SHIFL Reviewed; 280 AA.
AC P0A441; P38480;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Formyltetrahydrofolate deformylase {ECO:0000255|HAMAP-Rule:MF_01927};
DE EC=3.5.1.10 {ECO:0000255|HAMAP-Rule:MF_01927};
DE AltName: Full=Formyl-FH(4) hydrolase {ECO:0000255|HAMAP-Rule:MF_01927};
GN Name=purU {ECO:0000255|HAMAP-Rule:MF_01927};
GN OrderedLocusNames=SF1232, S1318;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=1406252; DOI=10.1111/j.1365-2958.1992.tb01385.x;
RA Hromockyj A.E., Tucker S.C., Maurelli A.T.;
RT "Temperature regulation of Shigella virulence: identification of the
RT repressor gene virR, an analogue of hns, and partial complementation by
RT tyrosyl transfer RNA (tRNA1(Tyr)).";
RL Mol. Microbiol. 6:2113-2124(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [4]
RP IDENTIFICATION.
RX PubMed=8226647; DOI=10.1128/jb.175.21.7066-7073.1993;
RA Nagy P.L., McCorkle G., Zalkin H.;
RT "purU, a source of formate for purT-dependent phosphoribosyl-N-
RT formylglycinamide synthesis.";
RL J. Bacteriol. 175:7066-7073(1993).
CC -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate
CC (formyl-FH4) to formate and tetrahydrofolate (FH4). {ECO:0000255|HAMAP-
CC Rule:MF_01927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + H2O = (6S)-5,6,7,8-
CC tetrahydrofolate + formate + H(+); Xref=Rhea:RHEA:19833,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57454; EC=3.5.1.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01927};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC formate from 10-formyl-5,6,7,8-tetrahydrofolate: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01927}.
CC -!- SIMILARITY: Belongs to the PurU family. {ECO:0000255|HAMAP-
CC Rule:MF_01927}.
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DR EMBL; X66849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE005674; AAN42845.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16730.1; -; Genomic_DNA.
DR RefSeq; NP_707138.1; NC_004337.2.
DR RefSeq; WP_000555849.1; NZ_WPGW01000029.1.
DR AlphaFoldDB; P0A441; -.
DR SMR; P0A441; -.
DR STRING; 198214.SF1232; -.
DR DNASU; 1079475; -.
DR EnsemblBacteria; AAN42845; AAN42845; SF1232.
DR EnsemblBacteria; AAP16730; AAP16730; S1318.
DR GeneID; 1024168; -.
DR GeneID; 66674946; -.
DR KEGG; sfl:SF1232; -.
DR KEGG; sfx:S1318; -.
DR PATRIC; fig|198214.7.peg.1450; -.
DR HOGENOM; CLU_038395_3_2_6; -.
DR OMA; HADHHTD; -.
DR OrthoDB; 979667at2; -.
DR UniPathway; UPA00074; UER00170.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04875; ACT_F4HF-DF; 1.
DR CDD; cd08648; FMT_core_Formyl-FH4-Hydrolase_C; 1.
DR HAMAP; MF_01927; PurU; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR041729; Formyl-FH4-Hydrolase_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR004810; PurU.
DR InterPro; IPR044074; PurU_ACT.
DR PANTHER; PTHR42706; PTHR42706; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR PRINTS; PR01575; FFH4HYDRLASE.
DR SUPFAM; SSF53328; SSF53328; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR00655; PurU; 1.
DR PROSITE; PS51671; ACT; 1.
PE 3: Inferred from homology;
KW Hydrolase; One-carbon metabolism; Purine biosynthesis; Reference proteome.
FT CHAIN 1..280
FT /note="Formyltetrahydrofolate deformylase"
FT /id="PRO_0000074966"
FT DOMAIN 8..86
FT /note="ACT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01927"
FT ACT_SITE 225
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01927"
FT CONFLICT 44
FT /note="R -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31921 MW; 55BC16B62727A419 CRC64;
MHSLQRKVLR TICPDQKGLI ARITNICYKH ELNIVQNNEF VDHRTGRFFM RTELEGIFND
STLLADLDSA LPEGSVRELN PAGRRRIVIL VTKEAHCLGD LLMKANYGGL DVEIAAVIGN
HDTLRSLVER FDIPFELVSH EGLSRNEHDQ KMADAIDAYQ PDYVVLAKYM RVLTPEFVAR
FPNKIINIHH SFLPAFIGAR PYHQAYERGV KIIGATAHYV NDNLDEGPII MQDVIHVDHT
YTAEDMMRAG RDVEKNVLSR ALYKVLAQRV FVYGNRTIIL
