USHA_ECOLI
ID USHA_ECOLI Reviewed; 550 AA.
AC P07024; P78274; Q2MBU7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Protein UshA;
DE Includes:
DE RecName: Full=UDP-sugar hydrolase;
DE EC=3.6.1.45;
DE AltName: Full=UDP-sugar diphosphatase;
DE AltName: Full=UDP-sugar pyrophosphatase;
DE Includes:
DE RecName: Full=5'-nucleotidase;
DE Short=5'-NT;
DE EC=3.1.3.5;
DE Flags: Precursor;
GN Name=ushA; OrderedLocusNames=b0480, JW0469;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-27.
RX PubMed=3012467; DOI=10.1093/nar/14.10.4325;
RA Burns D.M., Beacham I.R.;
RT "Nucleotide sequence and transcriptional analysis of the E. coli ushA gene,
RT encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase): regulation of
RT the ushA gene, and the signal sequence of its encoded protein product.";
RL Nucleic Acids Res. 14:4325-4342(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 1-41.
RC STRAIN=K12 / DH5-alpha;
RA Fujisaki S., Ohnuma S., Horiuchi T., Takahashi I., Tsukui S., Nishimura Y.,
RA Nishino T., Inokuchi H.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 26-37.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 26-550.
RX PubMed=10331872; DOI=10.1038/8253;
RA Knoefel T., Straeter N.;
RT "X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase
RT containing a dimetal catalytic site.";
RL Nat. Struct. Biol. 6:448-453(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; PRODUCT
RP AND INHIBITOR.
RX PubMed=11491293; DOI=10.1006/jmbi.2001.4656;
RA Knoefel T., Straeter N.;
RT "Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-
RT nucleotidase based on crystal structures.";
RL J. Mol. Biol. 309:239-254(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RX PubMed=11491294; DOI=10.1006/jmbi.2001.4657;
RA Knoefel T., Straeter N.;
RT "E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation
RT resembling a ball-and-socket motion.";
RL J. Mol. Biol. 309:255-266(2001).
CC -!- FUNCTION: Degradation of external UDP-glucose to uridine monophosphate
CC and glucose-1-phosphate, which can then be used by the cell.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.;
CC EC=3.6.1.45;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- ACTIVITY REGULATION: The activity of this protein is inhibited by an
CC intracellular protein inhibitor.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11491293,
CC ECO:0000269|PubMed:11491294}.
CC -!- SUBCELLULAR LOCATION: Periplasm. Note=Exported from the cell, except a
CC small proportion that is internally localized.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; X03895; CAA27532.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40234.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73582.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76259.1; -; Genomic_DNA.
DR EMBL; D73370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G64778; YXECUG.
DR RefSeq; NP_415013.1; NC_000913.3.
DR RefSeq; WP_000771748.1; NZ_LN832404.1.
DR PDB; 1HO5; X-ray; 2.10 A; A/B=26-550.
DR PDB; 1HP1; X-ray; 1.70 A; A=26-550.
DR PDB; 1HPU; X-ray; 1.85 A; A/B/C/D=26-550.
DR PDB; 1OI8; X-ray; 2.10 A; A/B=26-550.
DR PDB; 1OID; X-ray; 2.10 A; A/B=26-550.
DR PDB; 1OIE; X-ray; 2.33 A; A=26-550.
DR PDB; 1USH; X-ray; 1.73 A; A=1-550.
DR PDB; 2USH; X-ray; 2.22 A; A/B=1-550.
DR PDB; 4WWL; X-ray; 2.23 A; A=26-550.
DR PDBsum; 1HO5; -.
DR PDBsum; 1HP1; -.
DR PDBsum; 1HPU; -.
DR PDBsum; 1OI8; -.
DR PDBsum; 1OID; -.
DR PDBsum; 1OIE; -.
DR PDBsum; 1USH; -.
DR PDBsum; 2USH; -.
DR PDBsum; 4WWL; -.
DR AlphaFoldDB; P07024; -.
DR SMR; P07024; -.
DR BioGRID; 4259843; 37.
DR DIP; DIP-11096N; -.
DR IntAct; P07024; 10.
DR STRING; 511145.b0480; -.
DR DrugBank; DB03148; Adenosine 5'-methylenediphosphate.
DR jPOST; P07024; -.
DR PaxDb; P07024; -.
DR PRIDE; P07024; -.
DR EnsemblBacteria; AAC73582; AAC73582; b0480.
DR EnsemblBacteria; BAE76259; BAE76259; BAE76259.
DR GeneID; 947331; -.
DR KEGG; ecj:JW0469; -.
DR KEGG; eco:b0480; -.
DR PATRIC; fig|1411691.4.peg.1796; -.
DR EchoBASE; EB1053; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_7_0_6; -.
DR InParanoid; P07024; -.
DR OMA; VQPFTNM; -.
DR PhylomeDB; P07024; -.
DR BioCyc; EcoCyc:USHA-MON; -.
DR BioCyc; MetaCyc:USHA-MON; -.
DR BRENDA; 3.1.3.5; 2026.
DR SABIO-RK; P07024; -.
DR EvolutionaryTrace; P07024; -.
DR PRO; PR:P07024; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Nucleotide-binding; Periplasm; Reference proteome; Signal;
KW Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:3012467,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 26..550
FT /note="Protein UshA"
FT /id="PRO_0000000031"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 375..379
FT /ligand="substrate"
FT BINDING 498..504
FT /ligand="substrate"
FT SITE 117
FT /note="Transition state stabilizer"
FT SITE 120
FT /note="Transition state stabilizer"
FT DISULFID 258..275
FT CONFLICT 256
FT /note="P -> T (in Ref. 1; CAA27532)"
FT /evidence="ECO:0000305"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 56..73
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1HP1"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:1HP1"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:1HP1"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:1HPU"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 293..303
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 306..318
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:1HPU"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1OID"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 343..359
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 420..426
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 440..450
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 461..471
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 489..496
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:1HO5"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 522..533
FT /evidence="ECO:0007829|PDB:1HP1"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:1HP1"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:1HP1"
SQ 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
