PURNU_SHIFL
ID PURNU_SHIFL Reviewed; 243 AA.
AC A0A384KG77; A0A2S4MZ83; Q7C0D7; Q83K13;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Purine nucleoside phosphorylase YfiH;
DE EC=2.4.2.1 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=Adenosine deaminase YfiH;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=S-methyl-5'-thioadenosine phosphorylase YfiH;
DE EC=2.4.2.28 {ECO:0000250|UniProtKB:P84138};
GN Name=yfiH; OrderedLocusNames=SF2654;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
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 [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ZINC.
RA Seetharaman J., Swaminathan S.;
RT "Crystal Structure of Conserved Hypothetical Protein.";
RL Submitted (JUL-2004) to the PDB data bank.
RN [3] {ECO:0007744|PDB:1XAF}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=16498617; DOI=10.1002/prot.20589;
RA Kim Y., Maltseva N., Dementieva I., Collart F., Holzle D., Joachimiak A.;
RT "Crystal structure of hypothetical protein YfiH from Shigella flexneri at 2
RT A resolution.";
RL Proteins 63:1097-1101(2006).
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. Also catalyzes the
CC phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-
CC 5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase
CC activity. {ECO:0000250|UniProtKB:P84138}.
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:0000250|UniProtKB:P84138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643;
CC Evidence={ECO:0000250|UniProtKB:P84138};
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:0000250|UniProtKB:P84138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853;
CC Evidence={ECO:0000250|UniProtKB:P84138};
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:0000250|UniProtKB:P84138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647;
CC Evidence={ECO:0000250|UniProtKB:P84138};
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:0000250|UniProtKB:P84138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC -!- SIMILARITY: Belongs to the purine nucleoside phosphorylase YfiH/LACC1
CC family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44150.1; -; Genomic_DNA.
DR RefSeq; NP_708443.1; NC_004337.2.
DR RefSeq; WP_000040142.1; NZ_WPGW01000198.1.
DR PDB; 1U05; X-ray; 2.50 A; A/B=1-243.
DR PDB; 1XAF; X-ray; 2.01 A; A/B=1-243.
DR PDBsum; 1U05; -.
DR PDBsum; 1XAF; -.
DR AlphaFoldDB; A0A384KG77; -.
DR SMR; A0A384KG77; -.
DR EnsemblBacteria; AAN44150; AAN44150; SF2654.
DR GeneID; 1027284; -.
DR GeneID; 58391810; -.
DR KEGG; sfl:SF2654; -.
DR PATRIC; fig|198214.7.peg.3163; -.
DR HOGENOM; CLU_065784_1_1_6; -.
DR OMA; CFADCVP; -.
DR OrthoDB; 1393323at2; -.
DR Proteomes; UP000001006; Chromosome.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-EC.
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_0000449803"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16498617, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1U05, ECO:0007744|PDB:1XAF"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16498617, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1U05, ECO:0007744|PDB:1XAF"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16498617, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1U05, ECO:0007744|PDB:1XAF"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:1XAF"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1U05"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 99..114
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1XAF"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:1XAF"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:1XAF"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1XAF"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1XAF"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:1XAF"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:1XAF"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1XAF"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1XAF"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1XAF"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:1XAF"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1XAF"
SQ SEQUENCE 243 AA; 26380 MW; D3608345B3426269 CRC64;
MSKLIVPQWP LPKGVAACSS TRIGGVSLPP YDSLNLGAHC GDNPDHVEEN RKRLFAAGNL
PSKPVWLEQV HGKDVLKLTG EPYASKRADA SYSNTPGTVC AVMTADCLPV LFCNRAGTEV
AAVHAGWRGL CAGVLEETVS CFADKPENIL AWLGPAIGPR AFEVGAEVRE AFMAVDAKAS
AAFIQHGDKY LADIYQLARQ RLANVGVEQI FGGDRCTYTE NETFFSYRRD KTTGRMASFI
WLI
