PURNU_ECOLI
ID PURNU_ECOLI Reviewed; 243 AA.
AC P33644; Q46989;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Purine nucleoside phosphorylase YfiH {ECO:0000305};
DE EC=2.4.2.1 {ECO:0000269|PubMed:31978345};
DE AltName: Full=Adenosine deaminase YfiH {ECO:0000305};
DE EC=3.5.4.4 {ECO:0000269|PubMed:31978345};
DE AltName: Full=Polyphenol oxidase YfiH {ECO:0000303|PubMed:16740638};
DE EC=1.10.3.- {ECO:0000269|PubMed:16740638};
DE AltName: Full=S-methyl-5'-thioadenosine phosphorylase YfiH {ECO:0000305};
DE EC=2.4.2.28 {ECO:0000269|PubMed:31978345};
GN Name=yfiH {ECO:0000303|PubMed:16740638, ECO:0000312|EMBL:AAC75642.1};
GN OrderedLocusNames=b2593, JW2575;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Ogura T., Tomoyasu T.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1906060; DOI=10.1128/jb.173.14.4247-4253.1991;
RA Kitagawa M., Wada C., Yoshioka S., Yura T.;
RT "Expression of ClpB, an analog of the ATP-dependent protease regulatory
RT subunit in Escherichia coli, is controlled by a heat shock sigma factor
RT (sigma 32).";
RL J. Bacteriol. 173:4247-4253(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-243.
RX PubMed=2066329; DOI=10.1128/jb.173.14.4254-4262.1991;
RA Squires C.L., Pedersen S., Ross B.M., Squires C.;
RT "ClpB is the Escherichia coli heat shock protein F84.1.";
RL J. Bacteriol. 173:4254-4262(1991).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=16740638; DOI=10.1074/jbc.m600577200;
RA Beloqui A., Pita M., Polaina J., Martinez-Arias A., Golyshina O.V.,
RA Zumarraga M., Yakimov M.M., Garcia-Arellano H., Alcalde M., Fernandez V.M.,
RA Elborough K., Andreu J.M., Ballesteros A., Plou F.J., Timmis K.N.,
RA Ferrer M., Golyshin P.N.;
RT "Novel polyphenol oxidase mined from a metagenome expression library of
RT bovine rumen: biochemical properties, structural analysis, and phylogenetic
RT relationships.";
RL J. Biol. Chem. 281:22933-22942(2006).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=20065048; DOI=10.1128/aac.00906-09;
RA Liu A., Tran L., Becket E., Lee K., Chinn L., Park E., Tran K.,
RA Miller J.H.;
RT "Antibiotic sensitivity profiles determined with an Escherichia coli gene
RT knockout collection: generating an antibiotic bar code.";
RL Antimicrob. Agents Chemother. 54:1393-1403(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
RC STRAIN=K12;
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of hypothetical UPF0124 protein yfiH (NP_417084.1) from
RT Escherichia coli K12 at 1.54 A resolution.";
RL Submitted (MAY-2005) to the PDB data bank.
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31978345; DOI=10.1016/j.cell.2019.12.017;
RA Cader M.Z., de Almeida Rodrigues R.P., West J.A., Sewell G.W.,
RA Md-Ibrahim M.N., Reikine S., Sirago G., Unger L.W., Inglesias-Romero A.B.,
RA Ramshorn K., Haag L.M., Saveljeva S., Ebel J.F., Rosenstiel P.,
RA Kaneider N.C., Lee J.C., Lawley T.D., Bradley A., Dougan G., Modis Y.,
RA Griffin J.L., Kaser A.;
RT "FAMIN is a multifunctional purine enzyme enabling the purine nucleotide
RT cycle.";
RL Cell 180:278-295(2020).
CC -!- FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of
CC adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and
CC the respective free bases, adenine and hypoxanthine (PubMed:31978345).
CC Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into
CC adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate
CC (PubMed:31978345). Also has adenosine deaminase activity
CC (PubMed:31978345). May also act as a polyphenol oxidase: able to
CC oxidize syringaldazine and 2,2'-azino-bis(3-ethylbenzthiazoline-6-
CC sulfonic acid) (ABTS) in vitro (PubMed:16740638).
CC {ECO:0000269|PubMed:16740638, ECO:0000269|PubMed:31978345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate;
CC Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000269|PubMed:31978345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643;
CC Evidence={ECO:0000269|PubMed:31978345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58533; EC=2.4.2.28;
CC Evidence={ECO:0000269|PubMed:31978345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853;
CC Evidence={ECO:0000269|PubMed:31978345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate +
CC hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000269|PubMed:31978345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647;
CC Evidence={ECO:0000269|PubMed:31978345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000269|PubMed:31978345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000269|PubMed:31978345};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:16740638};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid (at
CC pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638};
CC KM=1.10 uM for syringaldazine (at pH 4.5 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:16740638};
CC Note=kcat is 1450 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-
CC 6-sulfonic acid as substrate. kcat is 21720 min(-1) with
CC syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).
CC {ECO:0000269|PubMed:16740638};
CC pH dependence:
CC Optimum pH is 5.5-8.4. Maintains 80% activity at pH 5.0-9.0.
CC {ECO:0000269|PubMed:16740638};
CC Temperature dependence:
CC Optimum temperature is 44 degrees Celsius. Maintains more than 80%
CC activity at 50 degrees Celsius. {ECO:0000269|PubMed:16740638};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16740638}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are more sensitive to
CC ampicillin, cephradine and cefoxitin than wild-type.
CC {ECO:0000269|PubMed:20065048}.
CC -!- SIMILARITY: Belongs to the purine nucleoside phosphorylase YfiH/LACC1
CC family. {ECO:0000305}.
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DR EMBL; U50134; AAA92958.1; -; Genomic_DNA.
DR EMBL; X57620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC75642.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16477.1; -; Genomic_DNA.
DR EMBL; M29364; AAA24421.1; ALT_SEQ; Genomic_DNA.
DR PIR; D65037; D65037.
DR RefSeq; NP_417084.1; NC_000913.3.
DR RefSeq; WP_000040169.1; NZ_LN832404.1.
DR PDB; 1Z9T; X-ray; 1.54 A; A=1-243.
DR PDB; 7F3V; X-ray; 1.47 A; A/B/C/D=1-243.
DR PDB; 7W1G; X-ray; 1.86 A; A/B/C/D=1-243.
DR PDBsum; 1Z9T; -.
DR PDBsum; 7F3V; -.
DR PDBsum; 7W1G; -.
DR AlphaFoldDB; P33644; -.
DR SMR; P33644; -.
DR BioGRID; 4260619; 654.
DR IntAct; P33644; 8.
DR STRING; 511145.b2593; -.
DR DrugBank; DB04272; Citric acid.
DR jPOST; P33644; -.
DR PaxDb; P33644; -.
DR PRIDE; P33644; -.
DR DNASU; 947089; -.
DR EnsemblBacteria; AAC75642; AAC75642; b2593.
DR EnsemblBacteria; BAA16477; BAA16477; BAA16477.
DR GeneID; 947089; -.
DR KEGG; ecj:JW2575; -.
DR KEGG; eco:b2593; -.
DR PATRIC; fig|511145.12.peg.2693; -.
DR EchoBASE; EB2021; -.
DR eggNOG; COG1496; Bacteria.
DR HOGENOM; CLU_065784_1_1_6; -.
DR InParanoid; P33644; -.
DR OMA; CFADCVP; -.
DR PhylomeDB; P33644; -.
DR BioCyc; EcoCyc:EG12097-MON; -.
DR BioCyc; MetaCyc:EG12097-MON; -.
DR SABIO-RK; P33644; -.
DR EvolutionaryTrace; P33644; -.
DR PRO; PR:P33644; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004000; F:adenosine deaminase activity; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IDA:UniProtKB.
DR CDD; cd16833; YfiH; 1.
DR Gene3D; 3.60.140.10; -; 1.
DR InterPro; IPR003730; Cu_polyphenol_OxRdtase.
DR InterPro; IPR038371; Cu_polyphenol_OxRdtase_sf.
DR InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat.
DR PANTHER; PTHR30616; PTHR30616; 1.
DR Pfam; PF02578; Cu-oxidase_4; 1.
DR SUPFAM; SSF64438; SSF64438; 1.
DR TIGRFAMs; TIGR00726; TIGR00726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Hydrolase; Metal-binding; Oxidoreductase;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..243
FT /note="Purine nucleoside phosphorylase YfiH"
FT /id="PRO_0000163163"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
FT CONFLICT 27
FT /note="S -> T (in Ref. 1; AAA92958)"
FT /evidence="ECO:0000305"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:7F3V"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:7W1G"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:7F3V"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 99..114
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:7F3V"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:7F3V"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:7F3V"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:7F3V"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7F3V"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:7F3V"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:7F3V"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:7F3V"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:7F3V"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:7F3V"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:7F3V"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:7F3V"
SQ SEQUENCE 243 AA; 26339 MW; D21267A5374EAC43 CRC64;
MSKLIVPQWP QPKGVAACSS TRIGGVSLPP YDSLNLGAHC GDNPDHVEEN RKRLFAAGNL
PSKPVWLEQV HGKDVLKLTG EPYASKRADA SYSNTPGTVC AVMTADCLPV LFCNRAGTEV
AAAHAGWRGL CAGVLEETVS CFADNPENIL AWLGPAIGPR AFEVGGEVRE AFMAVDAKAS
AAFIQHGDKY LADIYQLARQ RLANVGVEQI FGGDRCTYTE NETFFSYRRD KTTGRMASFI
WLI
