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   27-MAR-2024, entry version 211.
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; Pseudomonadota; 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; 511145-b0480; -.
DR   EnsemblBacteria; AAC73582; AAC73582; b0480.
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; NYDCDSP; -.
DR   OrthoDB; 9803927at2; -.
DR   PhylomeDB; P07024; -.
DR   BioCyc; EcoCyc:USHA-MONOMER; -.
DR   BioCyc; MetaCyc:USHA-MONOMER; -.
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; IEA:InterPro.
DR   CDD; cd07405; MPP_UshA_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 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; 5'-NUCLEOTIDASE-RELATED; 1.
DR   PANTHER; PTHR11575:SF46; PROTEIN USHA; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 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
//