Reviewed, UniProtKB/Swiss-Prot P0AE12 (AMN_ECOLI)

Names and origin

Protein names

Recommended name:
    AMP nucleosidase
    EC=3.2.2.4

Gene names

Name:	amn
Ordered Locus Names:	b1982, JW1963

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in regulation of AMP concentrations.
Catalytic activity	AMP + H2O = D-ribose 5-phosphate + adenine.
Enzyme regulation	Allosterically activated by Mg-ATP, and inactivated by inorganic phosphate.
Pathway	Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Induction	By cAMP at limiting phosphate concentrations. Repressed by phosphate.
Miscellaneous	AMP nucleosidase binds AMP at the catalytic site, Mg-ATP at an allosteric regulatory site, and inorganic phosphate also at a regulatory site.

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	AMP nucleosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 484

484

AMP nucleosidase

PRO_0000064586

Experimental info

Sequence conflict

300 – 302

3

WLM → CY in AAA23433. Ref.1

Sequence conflict

311 – 316

6

ESQAIG → KVRPLA in AAA23433. Ref.1

Secondary structure

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484

Helix Strand Turn

Details...

Helix

10 – 37

28

Helix

44 – 48

5

Turn

49 – 52

4

Beta strand

53 – 61

9

Beta strand

73 – 75

3

Beta strand

78 – 86

9

Turn

90 – 93

4

Helix

94 – 108

15

Beta strand

111 – 120

10

Helix

123 – 125

3

Helix

136 – 145

10

Beta strand

169 – 174

6

Helix

176 – 190

15

Helix

194 – 196

3

Beta strand

199 – 206

8

Helix

207 – 222

16

Beta strand

226 – 233

8

Beta strand

238 – 240

3

Turn

246 – 249

4

Helix

254 – 257

4

Beta strand

262 – 267

6

Beta strand

273 – 277

5

Helix

282 – 292

11

Helix

293 – 295

3

Beta strand

298 – 302

5

Beta strand

305 – 308

4

Beta strand

318 – 327

10

Turn

330 – 334

5

Helix

345 – 359

15

Turn

362 – 364

3

Helix

365 – 368

4

Beta strand

370 – 379

10

Helix

383 – 386

4

Helix

387 – 396

10

Beta strand

399 – 405

7

Helix

406 – 416

11

Beta strand

420 – 429

10

Helix

430 – 432

3

Helix

443 – 446

4

Helix

449 – 465

17

Helix

467 – 470

4

Helix

473 – 475

3

Sequences

	Sequence		Length	Mass (Da)
	P0AE12-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: ADC2FD95CC220527	FASTA	484	53,995
	10 20 30 40 50 60 MNNKGSGLTP AQALDKLDAL YEQSVVALRN AIGNYITSGE LPDENARKQG LFVYPSLTVT 70 80 90 100 110 120 WDGSTTNPPK TRAFGRFTHA GSYTTTITRP TLFRSYLNEQ LTLLYQDYGA HISVQPSQHE 130 140 150 160 170 180 IPYPYVIDGS ELTLDRSMSA GLTRYFPTTE LAQIGDETAD GIYHPTEFSP LSHFDARRVD 190 200 210 220 230 240 FSLARLRHYT GTPVEHFQPF VLFTNYTRYV DEFVRWGCSQ ILDPDSPYIA LSCAGGNWIT 250 260 270 280 290 300 AETEAPEEAI SDLAWKKHQM PAWHLITADG QGITLVNIGV GPSNAKTICD HLAVLRPDVW 310 320 330 340 350 360 LMIGHCGGLR ESQAIGDYVL AHAYLRDDHV LDAVLPPDIP IPSIAEVQRA LYDATKLVSG 370 380 390 400 410 420 RPGEEVKQRL RTGTVVTTDD RNWELRYSAS ALRFNLSRAV AIDMESATIA AQGYRFRVPY 430 440 450 460 470 480 GTLLCVSDKP LHGEIKLPGQ ANRFYEGAIS EHLQIGIRAI DLLRAEGDRL HSRKLRTFNE PPFR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and regulation of the AMP nucleosidase gene (amn) from Escherichia coli." Leung H.B., Kvalnes-Krick K.L., Meyer S.L., Deriel J.K., Schramm V.L. Biochemistry 28:8726-8733(1989) [PubMed: 2690948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Cloning and analysis of the shiA gene, which encodes the shikimate transport system of Escherichia coli K-12." Whipp M.J., Camakaris H., Pittard A.J. Gene 209:185-192(1998) [PubMed: 9524262] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M30469 Genomic DNA. Translation: AAA23433.1.
U00096 Genomic DNA. Translation: AAC75046.1.
AP009048 Genomic DNA. Translation: BAA15802.1.
U88529 Genomic DNA. Translation: AAC46272.1.

PIR

H64962.

RefSeq

AP_002586.1.
NP_416489.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T8R	X-ray	2.70	A/B/C/D/E/F	1-484	[»]
1T8S	X-ray	2.60	A/B/C/D/E/F	1-484	[»]
1T8W	X-ray	2.80	A/B/C/D/E/F	1-484	[»]
1T8Y	X-ray	3.00	A/B/C/D/E/F	1-484	[»]

ModBase

Search...

2-D gel databases

ECO2DBASE

G052.0. 6TH EDITION.

Genome annotation databases

GeneID

946508.

GenomeReviews

Gene locus JW1963 in contig AP009048_GR.
Gene locus b1982 in contig U00096_GR.

KEGG

ecj:JW1963.
eco:b1982.

Organism-specific databases

EchoBASE

EB0037.

EcoGene

EG10039. amn.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AE12.

OMA

P0AE12. WLMVGHC.

Enzyme and pathway databases

BioCyc

EcoCyc:AMP-NUCLEOSID-MON.
MetaCyc:AMP-NUCLEOSID-MON.

Family and domain databases

InterPro

IPR011271. AMP_nucleosidase.
IPR018953. AMP_nucleoside_Pase_N.
IPR000845. Nucleoside_phosphorylase.
IPR018017. Nucleoside_phosphorylase_1.
[Graphical view]

Gene3D

G3DSA:3.30.1730.10. AMP_nucleoside_Pase_N. 1 hit.

PANTHER

PTHR21234. PNP_UDP. 1 hit.

Pfam

PF10423. AMNp_N. 1 hit.
PF01048. PNP_UDP_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01717. AMP-nucleosdse. 1 hit.

ProtoNet

Search...

Entry information

Entry name

AMN_ECOLI

Accession

Primary (citable) accession number: P0AE12
Secondary accession number(s): P15272, P78074

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)