ID AMN_ECOLI Reviewed; 484 AA. AC P0AE12; P15272; P78074; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 24-JAN-2024, entry version 126. DE RecName: Full=AMP nucleosidase {ECO:0000255|HAMAP-Rule:MF_01932, ECO:0000303|PubMed:7000783}; DE EC=3.2.2.4 {ECO:0000255|HAMAP-Rule:MF_01932, ECO:0000269|PubMed:7000783}; GN Name=amn {ECO:0000255|HAMAP-Rule:MF_01932, GN ECO:0000303|PubMed:2690948}; GN OrderedLocusNames=b1982 {ECO:0000312|EMBL:AAC75046.1}, JW1963 GN {ECO:0000312|EMBL:BAA15802.1}; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND INDUCTION. RX PubMed=2690948; DOI=10.1021/bi00448a008; RA Leung H.B., Kvalnes-Krick K.L., Meyer S.L., Deriel J.K., Schramm V.L.; RT "Structure and regulation of the AMP nucleosidase gene (amn) from RT Escherichia coli."; RL Biochemistry 28:8726-8733(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., RA Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [3] 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159. RC STRAIN=K12; RX PubMed=9524262; DOI=10.1016/s0378-1119(98)00043-2; RA Whipp M.J., Camakaris H., Pittard A.J.; RT "Cloning and analysis of the shiA gene, which encodes the shikimate RT transport system of Escherichia coli K-12."; RL Gene 209:185-192(1998). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=K12; RX PubMed=7000783; DOI=10.1016/s0021-9258(19)70387-1; RA Leung H.B., Schramm V.L.; RT "Adenylate degradation in Escherichia coli. The role of AMP nucleosidase RT and properties of the purified enzyme."; RL J. Biol. Chem. 255:10867-10874(1980). RN [7] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [8] RP DISRUPTION PHENOTYPE. RX PubMed=18029299; DOI=10.1098/rsbl.2007.0432; RA Morrison B.A., Shain D.H.; RT "An AMP nucleosidase gene knockout in Escherichia coli elevates RT intracellular ATP levels and increases cold tolerance."; RL Biol. Lett. 4:53-56(2008). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RP FORMYCIN-5'-MONOPHOSPHATE AND PHOSPHATE, SUBUNIT, AND DOMAIN. RX PubMed=15296732; DOI=10.1016/j.str.2004.05.015; RA Zhang Y., Cottet S.E., Ealick S.E.; RT "Structure of Escherichia coli AMP nucleosidase reveals similarity to RT nucleoside phosphorylases."; RL Structure 12:1383-1394(2004). CC -!- FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond of AMP to CC form adenine and ribose 5-phosphate. Involved in regulation of AMP CC concentrations. {ECO:0000255|HAMAP-Rule:MF_01932, CC ECO:0000269|PubMed:7000783}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + H2O = adenine + D-ribose 5-phosphate; CC Xref=Rhea:RHEA:20129, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.2.2.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01932, CC ECO:0000269|PubMed:7000783}; CC -!- ACTIVITY REGULATION: Allosterically activated by Mg-ATP. Inhibited by CC inorganic phosphate and formycin monophosphate. CC {ECO:0000269|PubMed:7000783}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=15 mM for AMP (in the absence of Mg-ATP) CC {ECO:0000269|PubMed:7000783}; CC KM=0.09 mM for AMP (in the presence of saturating Mg-ATP) CC {ECO:0000269|PubMed:7000783}; CC -!- SUBUNIT: Homohexamer. Trimer of dimers. {ECO:0000269|PubMed:15296732}. CC -!- INDUCTION: By cAMP at limiting phosphate concentrations. Repressed by CC phosphate. {ECO:0000269|PubMed:2690948}. CC -!- DOMAIN: Each monomer consists of two domains: a C-terminal catalytic CC domain and a putative N-terminal regulatory domain. CC {ECO:0000269|PubMed:15296732}. CC -!- DISRUPTION PHENOTYPE: Knockout elevates intracellular ATP levels and CC increases cold tolerance. {ECO:0000269|PubMed:18029299}. CC -!- MISCELLANEOUS: AMP nucleosidase binds AMP at the catalytic site, Mg-ATP CC at an allosteric regulatory site, and inorganic phosphate also at a CC regulatory site. {ECO:0000303|PubMed:2690948}. CC -!- SIMILARITY: Belongs to the AMP nucleosidase family. {ECO:0000255|HAMAP- CC Rule:MF_01932, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M30469; AAA23433.1; -; Genomic_DNA. DR EMBL; U00096; AAC75046.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15802.1; -; Genomic_DNA. DR EMBL; U88529; AAC46272.1; -; Genomic_DNA. DR PIR; H64962; H64962. DR RefSeq; NP_416489.1; NC_000913.3. DR RefSeq; WP_001060244.1; NZ_SSTT01000011.1. DR PDB; 1T8R; X-ray; 2.70 A; A/B/C/D/E/F=1-484. DR PDB; 1T8S; X-ray; 2.60 A; A/B/C/D/E/F=1-484. DR PDB; 1T8W; X-ray; 2.80 A; A/B/C/D/E/F=1-484. DR PDB; 1T8Y; X-ray; 3.00 A; A/B/C/D/E/F=1-484. DR PDBsum; 1T8R; -. DR PDBsum; 1T8S; -. DR PDBsum; 1T8W; -. DR PDBsum; 1T8Y; -. DR AlphaFoldDB; P0AE12; -. DR SMR; P0AE12; -. DR BioGRID; 4260401; 10. DR IntAct; P0AE12; 8. DR STRING; 511145.b1982; -. DR DrugBank; DB03464; Formycin-5'-Monophosphate. DR jPOST; P0AE12; -. DR PaxDb; 511145-b1982; -. DR EnsemblBacteria; AAC75046; AAC75046; b1982. DR GeneID; 75202785; -. DR GeneID; 946508; -. DR KEGG; ecj:JW1963; -. DR KEGG; eco:b1982; -. DR PATRIC; fig|1411691.4.peg.269; -. DR EchoBASE; EB0037; -. DR eggNOG; COG0775; Bacteria. DR HOGENOM; CLU_026838_1_0_6; -. DR InParanoid; P0AE12; -. DR OMA; RPHAWIM; -. DR OrthoDB; 7945729at2; -. DR PhylomeDB; P0AE12; -. DR BioCyc; EcoCyc:AMP-NUCLEOSID-MONOMER; -. DR BioCyc; MetaCyc:AMP-NUCLEOSID-MONOMER; -. DR EvolutionaryTrace; P0AE12; -. DR PRO; PR:P0AE12; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0008714; F:AMP nucleosidase activity; IDA:EcoCyc. DR GO; GO:0044209; P:AMP salvage; IEA:InterPro. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR CDD; cd17762; AMN; 1. DR Gene3D; 3.30.1730.10; AMP nucleoside phosphorylase, N-terminal domain; 1. DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1. DR HAMAP; MF_01932; AMP_nucleosidase; 1. DR InterPro; IPR047039; AMN_phosphorylase. DR InterPro; IPR037109; AMP_N_sf. DR InterPro; IPR011271; AMP_nucleosidase. DR InterPro; IPR018953; AMP_nucleoside_Pase_N. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR035994; Nucleoside_phosphorylase_sf. DR NCBIfam; TIGR01717; AMP-nucleosdse; 1. DR PANTHER; PTHR43691:SF6; AMP NUCLEOSIDASE; 1. DR PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1. DR Pfam; PF10423; AMNp_N; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Direct protein sequencing; Hydrolase; KW Reference proteome. FT CHAIN 1..484 FT /note="AMP nucleosidase" FT /id="PRO_0000064586" FT CONFLICT 300..302 FT /note="WLM -> CY (in Ref. 1; AAA23433)" FT /evidence="ECO:0000305" FT CONFLICT 311..316 FT /note="ESQAIG -> KVRPLA (in Ref. 1; AAA23433)" FT /evidence="ECO:0000305" FT HELIX 10..38 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:1T8S" FT TURN 48..50 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 51..61 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 78..86 FT /evidence="ECO:0007829|PDB:1T8S" FT TURN 90..93 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 94..108 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 111..120 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 123..126 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 136..145 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 169..174 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 176..190 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 194..196 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 199..205 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 208..222 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 226..233 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 254..257 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 262..267 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 282..292 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 305..308 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 318..327 FT /evidence="ECO:0007829|PDB:1T8S" FT TURN 330..334 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 345..358 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 363..368 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 370..379 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 387..397 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 399..405 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 406..415 FT /evidence="ECO:0007829|PDB:1T8S" FT STRAND 420..428 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 430..432 FT /evidence="ECO:0007829|PDB:1T8R" FT HELIX 443..446 FT /evidence="ECO:0007829|PDB:1T8R" FT HELIX 448..465 FT /evidence="ECO:0007829|PDB:1T8S" FT TURN 466..470 FT /evidence="ECO:0007829|PDB:1T8S" FT HELIX 473..475 FT /evidence="ECO:0007829|PDB:1T8R" SQ SEQUENCE 484 AA; 53995 MW; ADC2FD95CC220527 CRC64; MNNKGSGLTP AQALDKLDAL YEQSVVALRN AIGNYITSGE LPDENARKQG LFVYPSLTVT WDGSTTNPPK TRAFGRFTHA GSYTTTITRP TLFRSYLNEQ LTLLYQDYGA HISVQPSQHE IPYPYVIDGS ELTLDRSMSA GLTRYFPTTE LAQIGDETAD GIYHPTEFSP LSHFDARRVD FSLARLRHYT GTPVEHFQPF VLFTNYTRYV DEFVRWGCSQ ILDPDSPYIA LSCAGGNWIT AETEAPEEAI SDLAWKKHQM PAWHLITADG QGITLVNIGV GPSNAKTICD HLAVLRPDVW LMIGHCGGLR ESQAIGDYVL AHAYLRDDHV LDAVLPPDIP IPSIAEVQRA LYDATKLVSG RPGEEVKQRL RTGTVVTTDD RNWELRYSAS ALRFNLSRAV AIDMESATIA AQGYRFRVPY GTLLCVSDKP LHGEIKLPGQ ANRFYEGAIS EHLQIGIRAI DLLRAEGDRL HSRKLRTFNE PPFR //