PURU_ECOLI
ID PURU_ECOLI Reviewed; 280 AA.
AC P37051;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 165.
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}; Synonyms=tgs, ychI;
GN OrderedLocusNames=b1232, JW1220;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-6.
RC STRAIN=K12;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8282700; DOI=10.1128/jb.176.1.221-231.1994;
RA Boesl M., Kersten H.;
RT "Organization and functions of genes in the upstream region of tyrT of
RT Escherichia coli: phenotypes of mutants with partial deletion of a new gene
RT (tgs).";
RL J. Bacteriol. 176:221-231(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RX PubMed=7868604; DOI=10.1128/jb.177.5.1292-1298.1995;
RA Nagy P.L., Marolewski A., Benkovic S.J., Zalkin H.;
RT "Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to
RT balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts
RT in Escherichia coli.";
RL J. Bacteriol. 177:1292-1298(1995).
CC -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate
CC (formyl-FH4) to formate and tetrahydrofolate (FH4). Provides the major
CC source of formate for the PurT-dependent synthesis of 5'-
CC phosphoribosyl-N-formylglycinamide (FGAR) during aerobic growth. Has a
CC role in regulating the one-carbon pool. {ECO:0000255|HAMAP-
CC Rule:MF_01927, ECO:0000269|PubMed:7868604}.
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 ECO:0000269|PubMed:7868604};
CC -!- ACTIVITY REGULATION: Activated by methionine, inhibited by glycine.
CC {ECO:0000269|PubMed:7868604}.
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, ECO:0000269|PubMed:7868604}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:7868604}.
CC -!- SIMILARITY: Belongs to the PurU family. {ECO:0000255|HAMAP-
CC Rule:MF_01927}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16860.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L20251; AAC36846.1; -; Unassigned_DNA.
DR EMBL; M64675; AAA16860.1; ALT_INIT; Unassigned_DNA.
DR EMBL; U00096; AAC74314.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36100.1; -; Genomic_DNA.
DR PIR; C36871; C36871.
DR RefSeq; NP_415748.1; NC_000913.3.
DR RefSeq; WP_000555857.1; NZ_SSZK01000031.1.
DR AlphaFoldDB; P37051; -.
DR SMR; P37051; -.
DR BioGRID; 4261924; 11.
DR IntAct; P37051; 3.
DR STRING; 511145.b1232; -.
DR jPOST; P37051; -.
DR PaxDb; P37051; -.
DR PRIDE; P37051; -.
DR DNASU; 945827; -.
DR EnsemblBacteria; AAC74314; AAC74314; b1232.
DR EnsemblBacteria; BAA36100; BAA36100; BAA36100.
DR GeneID; 945827; -.
DR KEGG; ecj:JW1220; -.
DR KEGG; eco:b1232; -.
DR PATRIC; fig|1411691.4.peg.1053; -.
DR EchoBASE; EB1766; -.
DR eggNOG; COG0788; Bacteria.
DR HOGENOM; CLU_038395_3_2_6; -.
DR InParanoid; P37051; -.
DR OMA; HADHHTD; -.
DR PhylomeDB; P37051; -.
DR BioCyc; EcoCyc:FORMYLTHFDEFORMYL-MON; -.
DR BioCyc; MetaCyc:FORMYLTHFDEFORMYL-MON; -.
DR BRENDA; 3.5.1.10; 2026.
DR UniPathway; UPA00074; UER00170.
DR PRO; PR:P37051; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IDA:EcoCyc.
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:0009257; P:10-formyltetrahydrofolate biosynthetic process; TAS:EcoCyc.
DR GO; GO:0006730; P:one-carbon metabolic process; TAS:EcoCyc.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:CACAO.
DR GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; One-carbon metabolism;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..280
FT /note="Formyltetrahydrofolate deformylase"
FT /id="PRO_0000074961"
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"
SQ SEQUENCE 280 AA; 31935 MW; 5667406D2727A2C2 CRC64;
MHSLQRKVLR TICPDQKGLI ARITNICYKH ELNIVQNNEF VDHRTGRFFM RTELEGIFND
STLLADLDSA LPEGSVRELN PAGRRRIVIL VTKEAHCLGD LLMKANYGGL DVEIAAVIGN
HDTLRSLVER FDIPFELVSH EGLTRNEHDQ KMADAIDAYQ PDYVVLAKYM RVLTPEFVAR
FPNKIINIHH SFLPAFIGAR PYHQAYERGV KIIGATAHYV NDNLDEGPII MQDVIHVDHT
YTAEDMMRAG RDVEKNVLSR ALYKVLAQRV FVYGNRTIIL
