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Protein UshA [Includes: UDP-sugar hydrolase (EC 3.6.1.45) (UDP-sugar diphosphatase) (UDP-sugar pyrophosphatase); 5'-nucleotidase (5'-NT) (EC 3.1.3.5)]

 USHA_ECOLI              Reviewed;         550 AA.
P07024; P78274; Q2MBU7;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
05-DEC-2018, entry version 186.
RecName: Full=Protein UshA;
Includes:
RecName: Full=UDP-sugar hydrolase;
EC=3.6.1.45;
AltName: Full=UDP-sugar diphosphatase;
AltName: Full=UDP-sugar pyrophosphatase;
Includes:
RecName: Full=5'-nucleotidase;
Short=5'-NT;
EC=3.1.3.5;
Flags: Precursor;
Name=ushA; OrderedLocusNames=b0480, JW0469;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-27.
PubMed=3012467; DOI=10.1093/nar/14.10.4325;
Burns D.M., Beacham I.R.;
"Nucleotide sequence and transcriptional analysis of the E. coli ushA
gene, encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase):
regulation of the ushA gene, and the signal sequence of its encoded
protein product.";
Nucleic Acids Res. 14:4325-4342(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
STRAIN=K12 / DH5-alpha;
Fujisaki S., Ohnuma S., Horiuchi T., Takahashi I., Tsukui S.,
Nishimura Y., Nishino T., Inokuchi H.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 26-37.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 26-550.
PubMed=10331872; DOI=10.1038/8253;
Knoefel T., Straeter N.;
"X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase
containing a dimetal catalytic site.";
Nat. Struct. Biol. 6:448-453(1999).
[8]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE;
PRODUCT AND INHIBITOR.
PubMed=11491293; DOI=10.1006/jmbi.2001.4656;
Knoefel T., Straeter N.;
"Mechanism of hydrolysis of phosphate esters by the dimetal center of
5'-nucleotidase based on crystal structures.";
J. Mol. Biol. 309:239-254(2001).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
PubMed=11491294; DOI=10.1006/jmbi.2001.4657;
Knoefel T., Straeter N.;
"E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation
resembling a ball-and-socket motion.";
J. Mol. Biol. 309:255-266(2001).
-!- FUNCTION: Degradation of external UDP-glucose to uridine
monophosphate and glucose-1-phosphate, which can then be used by
the cell.
-!- CATALYTIC ACTIVITY:
Reaction=UDP-sugar + H(2)O = UMP + alpha-D-aldose 1-phosphate.;
EC=3.6.1.45;
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043;
EC=3.1.3.5;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- ACTIVITY REGULATION: The activity of this protein is inhibited by
an intracellular protein inhibitor.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11491293,
ECO:0000269|PubMed:11491294}.
-!- SUBCELLULAR LOCATION: Periplasm. Note=Exported from the cell,
except a small proportion that is internally localized.
-!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X03895; CAA27532.1; -; Genomic_DNA.
EMBL; U82664; AAB40234.1; -; Genomic_DNA.
EMBL; U00096; AAC73582.1; -; Genomic_DNA.
EMBL; AP009048; BAE76259.1; -; Genomic_DNA.
EMBL; D73370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; G64778; YXECUG.
RefSeq; NP_415013.1; NC_000913.3.
RefSeq; WP_000771748.1; NZ_LN832404.1.
PDB; 1HO5; X-ray; 2.10 A; A/B=26-550.
PDB; 1HP1; X-ray; 1.70 A; A=26-550.
PDB; 1HPU; X-ray; 1.85 A; A/B/C/D=26-550.
PDB; 1OI8; X-ray; 2.10 A; A/B=26-550.
PDB; 1OID; X-ray; 2.10 A; A/B=26-550.
PDB; 1OIE; X-ray; 2.33 A; A=26-550.
PDB; 1USH; X-ray; 1.73 A; A=1-550.
PDB; 2USH; X-ray; 2.22 A; A/B=1-550.
PDB; 4WWL; X-ray; 2.23 A; A=26-550.
PDBsum; 1HO5; -.
PDBsum; 1HP1; -.
PDBsum; 1HPU; -.
PDBsum; 1OI8; -.
PDBsum; 1OID; -.
PDBsum; 1OIE; -.
PDBsum; 1USH; -.
PDBsum; 2USH; -.
PDBsum; 4WWL; -.
ProteinModelPortal; P07024; -.
SMR; P07024; -.
BioGrid; 4259843; 37.
DIP; DIP-11096N; -.
IntAct; P07024; 10.
STRING; 316385.ECDH10B_0436; -.
DrugBank; DB03148; Phosphomethylphosphonic Acid Adenosyl Ester.
EPD; P07024; -.
PaxDb; P07024; -.
PRIDE; P07024; -.
EnsemblBacteria; AAC73582; AAC73582; b0480.
EnsemblBacteria; BAE76259; BAE76259; BAE76259.
GeneID; 947331; -.
KEGG; ecj:JW0469; -.
KEGG; eco:b0480; -.
PATRIC; fig|1411691.4.peg.1796; -.
EchoBASE; EB1053; -.
EcoGene; EG11060; ushA.
eggNOG; ENOG4105CGH; Bacteria.
eggNOG; COG0737; LUCA.
HOGENOM; HOG000247216; -.
InParanoid; P07024; -.
KO; K11751; -.
PhylomeDB; P07024; -.
BioCyc; EcoCyc:USHA-MONOMER; -.
BioCyc; MetaCyc:USHA-MONOMER; -.
BRENDA; 3.1.3.5; 2026.
SABIO-RK; P07024; -.
EvolutionaryTrace; P07024; -.
PRO; PR:P07024; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0008253; F:5'-nucleotidase activity; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0008768; F:UDP-sugar diphosphatase activity; IDA:EcoCyc.
GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
Gene3D; 3.60.21.10; -; 1.
Gene3D; 3.90.780.10; -; 1.
InterPro; IPR008334; 5'-Nucleotdase_C.
InterPro; IPR036907; 5'-Nucleotdase_C_sf.
InterPro; IPR006146; 5'-Nucleotdase_CS.
InterPro; IPR006179; 5_nucleotidase/apyrase.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
PANTHER; PTHR11575; PTHR11575; 1.
Pfam; PF02872; 5_nucleotid_C; 1.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR01607; APYRASEFAMLY.
SUPFAM; SSF55816; SSF55816; 1.
PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Hydrolase; Metal-binding; Nucleotide-binding;
Periplasm; Reference proteome; Signal; Zinc.
SIGNAL 1 25 {ECO:0000269|PubMed:3012467,
ECO:0000269|PubMed:9298646}.
CHAIN 26 550 Protein UshA.
/FTId=PRO_0000000031.
REGION 375 379 Substrate binding.
REGION 498 504 Substrate binding.
METAL 41 41 Zinc 1.
METAL 43 43 Zinc 1.
METAL 84 84 Zinc 1.
METAL 84 84 Zinc 2.
METAL 116 116 Zinc 2.
METAL 217 217 Zinc 2.
METAL 252 252 Zinc 2.
METAL 254 254 Zinc 1.
SITE 117 117 Transition state stabilizer.
SITE 120 120 Transition state stabilizer.
DISULFID 258 275
CONFLICT 256 256 P -> T (in Ref. 1; CAA27532).
{ECO:0000305}.
STRAND 32 39 {ECO:0000244|PDB:1HP1}.
HELIX 56 73 {ECO:0000244|PDB:1HP1}.
STRAND 76 81 {ECO:0000244|PDB:1HP1}.
STRAND 86 88 {ECO:0000244|PDB:1HP1}.
HELIX 90 93 {ECO:0000244|PDB:1HP1}.
TURN 94 97 {ECO:0000244|PDB:1HP1}.
HELIX 98 107 {ECO:0000244|PDB:1HP1}.
STRAND 111 113 {ECO:0000244|PDB:1HP1}.
HELIX 116 119 {ECO:0000244|PDB:1HP1}.
HELIX 123 132 {ECO:0000244|PDB:1HP1}.
STRAND 140 144 {ECO:0000244|PDB:1HP1}.
TURN 145 147 {ECO:0000244|PDB:1HP1}.
STRAND 150 160 {ECO:0000244|PDB:1HP1}.
STRAND 163 171 {ECO:0000244|PDB:1HP1}.
TURN 173 177 {ECO:0000244|PDB:1HP1}.
STRAND 178 180 {ECO:0000244|PDB:1HP1}.
HELIX 181 184 {ECO:0000244|PDB:1HPU}.
STRAND 187 189 {ECO:0000244|PDB:1HP1}.
HELIX 192 206 {ECO:0000244|PDB:1HP1}.
STRAND 210 218 {ECO:0000244|PDB:1HP1}.
HELIX 222 224 {ECO:0000244|PDB:1HP1}.
HELIX 233 239 {ECO:0000244|PDB:1HP1}.
STRAND 244 249 {ECO:0000244|PDB:1HP1}.
STRAND 259 261 {ECO:0000244|PDB:1HP1}.
STRAND 278 280 {ECO:0000244|PDB:1HP1}.
STRAND 283 286 {ECO:0000244|PDB:1HP1}.
STRAND 293 303 {ECO:0000244|PDB:1HP1}.
STRAND 306 318 {ECO:0000244|PDB:1HP1}.
STRAND 320 324 {ECO:0000244|PDB:1HPU}.
STRAND 326 328 {ECO:0000244|PDB:1OID}.
STRAND 333 336 {ECO:0000244|PDB:1HP1}.
HELIX 343 359 {ECO:0000244|PDB:1HP1}.
STRAND 362 369 {ECO:0000244|PDB:1HP1}.
HELIX 375 378 {ECO:0000244|PDB:1HP1}.
HELIX 384 397 {ECO:0000244|PDB:1HP1}.
STRAND 400 405 {ECO:0000244|PDB:1HP1}.
HELIX 406 408 {ECO:0000244|PDB:1HP1}.
STRAND 415 419 {ECO:0000244|PDB:1HP1}.
HELIX 420 426 {ECO:0000244|PDB:1HP1}.
STRAND 432 439 {ECO:0000244|PDB:1HP1}.
HELIX 440 450 {ECO:0000244|PDB:1HP1}.
STRAND 455 457 {ECO:0000244|PDB:1HP1}.
STRAND 461 471 {ECO:0000244|PDB:1HP1}.
STRAND 474 480 {ECO:0000244|PDB:1HP1}.
STRAND 489 496 {ECO:0000244|PDB:1HP1}.
HELIX 497 500 {ECO:0000244|PDB:1HP1}.
HELIX 503 505 {ECO:0000244|PDB:1HP1}.
STRAND 512 514 {ECO:0000244|PDB:1HO5}.
STRAND 515 521 {ECO:0000244|PDB:1HP1}.
HELIX 522 533 {ECO:0000244|PDB:1HP1}.
HELIX 538 541 {ECO:0000244|PDB:1HP1}.
STRAND 545 550 {ECO:0000244|PDB:1HP1}.
SEQUENCE 550 AA; 60824 MW; DBA07B1C40C6C075 CRC64;
MKLLQRGVAL ALLTTFTLAS ETALAYEQDK TYKITVLHTN DHHGHFWRNE YGEYGLAAQK
TLVDGIRKEV AAEGGSVLLL SGGDINTGVP ESDLQDAEPD FRGMNLVGYD AMAIGNHEFD
NPLTVLRQQE KWAKFPLLSA NIYQKSTGER LFKPWALFKR QDLKIAVIGL TTDDTAKIGN
PEYFTDIEFR KPADEAKLVI QELQQTEKPD IIIAATHMGH YDNGEHGSNA PGDVEMARAL
PAGSLAMIVG GHSQDPVCMA AENKKQVDYV PGTPCKPDQQ NGIWIVQAHE WGKYVGRADF
EFRNGEMKMV NYQLIPVNLK KKVTWEDGKS ERVLYTPEIA ENQQMISLLS PFQNKGKAQL
EVKIGETNGR LEGDRDKVRF VQTNMGRLIL AAQMDRTGAD FAVMSGGGIR DSIEAGDISY
KNVLKVQPFG NVVVYADMTG KEVIDYLTAV AQMKPDSGAY PQFANVSFVA KDGKLNDLKI
KGEPVDPAKT YRMATLNFNA TGGDGYPRLD NKPGYVNTGF IDAEVLKAYI QKSSPLDVSV
YEPKGEVSWQ


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