AMN_ECOLI
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 03-AUG-2022, entry version 119.
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, ECO:0000303|PubMed:2690948};
GN OrderedLocusNames=b1982 {ECO:0000312|EMBL:AAC75046.1},
GN JW1963 {ECO:0000312|EMBL:BAA15802.1};
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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}.
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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; P0AE12; -.
DR PRIDE; P0AE12; -.
DR EnsemblBacteria; AAC75046; AAC75046; b1982.
DR EnsemblBacteria; BAA15802; BAA15802; BAA15802.
DR GeneID; 66674129; -.
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 PhylomeDB; P0AE12; -.
DR BioCyc; EcoCyc:AMP-NUCLEOSID-MON; -.
DR BioCyc; MetaCyc:AMP-NUCLEOSID-MON; -.
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 Gene3D; 3.30.1730.10; -; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR HAMAP; MF_01932; AMP_nucleosidase; 1.
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 PANTHER; PTHR43691:SF6; PTHR43691:SF6; 1.
DR Pfam; PF10423; AMNp_N; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01717; AMP-nucleosdse; 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
