Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.5: HAD, Beta-PGM, Phosphatase Like

  ⌊ C1.5.3: 5'-Nucleotidase Like

  ⌊ FunctionalDomain C1.5.3: 5'-Nucleotidase Like (ID 273581)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onJuly 22, 2015

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bos taurus Taxon ID: 9913 27806031 NP_776830.1 (RefSeq) PRP URP
Bison bison bison Taxon ID: 43346 742200436 XP_010857725.1 (RefSeq)
Bos grunniens mutus Taxon ID: 72004 555951818 XP_005888104.1 (RefSeq)
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Uniprot

Protein NameAccessionEC Number Identifier
Cytosolic purine 5'-nucleotidase O46411 3.1.3.5 5NTC_BOVIN (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 560 | Length of Functional Domain: 560

1       10        20        30        40        50        60

MTTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTVCDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEE
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues

Subgroup CAR This EFD conserves 1/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
249 Thr (T) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:21268116

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2JC9 Crystal Structure Of Human Cytosolic 5'-Nucleotidase Ii In Complex With Adenosine Cytosolic Purine 5'-Nucleotidase 19 1.5 Magnesium Ion
(3 more ⇓) 		CSA • PDB • PDBSum
2J2C Crystal Structure Of Human Cytosolic 5'-Nucleotidase Ii (Nt5C2, Cn-Ii) Cytosolic Purine 5'-Nucleotidase 19 2.2 Sulfate Ion
(2 more ⇓) 		CSA • PDB • PDBSum
4H4B Human Cytosolic 5'-Nucleotidase Ii In Complex With Anthraquinone-2,6-Disulfonic Acid Cytosolic Purine 5'-Nucleotidase 19 2.9 9,10-Dioxo-9,10-Dihydroanthracene-2,6-Disulfonic Acid
(3 more ⇓) 		CSA • PDB • PDBSum
2XJD Crystal Structure Of The D52N Variant Of Cytosolic 5'-Nucleotidase Ii In Complex With Inorganic Phosphate And Deoxyadenosine Triphosphate Cytosolic Purine 5'-Nucleotidase 17 2.0 Yes Adenosine-5'-Triphosphate
(3 more ⇓) 		CSA • PDB • PDBSum
2XJB Crystal Structure Of The D52N Variant Of Cytosolic 5'-Nucleotidase Ii In Complex With Deoxyguanosine Monophosphate And Deoxyadenosine Triphosphate Cytosolic Purine 5'-Nucleotidase 17 2.3 Yes Glycerol
(3 more ⇓) 		CSA • PDB • PDBSum
2XJC Crystal Structure Of The D52N Variant Of Cytosolic 5'-Nucleotidase Ii In Complex With Guanosine Monophosphate And Diadenosine Tetraphosphate Cytosolic Purine 5'-Nucleotidase 17 2.0 Yes Guanosine-5'-Monophosphate
(3 more ⇓) 		CSA • PDB • PDBSum
2XCW Crystal Structure Of The D52N Variant Of Cytosolic 5'-Nucleotidase Ii In Complex With Inosine Monophosphate And Atp Cytosolic Purine 5'-Nucleotidase 17 1.9 Yes Adenosine-5'-Triphosphate
(3 more ⇓) 		CSA • PDB • PDBSum
2XCV Crystal Structure Of The D52N Variant Of Cytosolic 5'-Nucleotidase Ii In Complex With Inosine Monophosphate And 2,3-Bisphosphoglycerate Cytosolic Purine 5'-Nucleotidase 17 2.3 Yes (2R)-2,3-Diphosphoglyceric Acid
(3 more ⇓) 		CSA • PDB • PDBSum
2XCX Crystal Structure Of The Apoform Of The D52N Variant Of Cytosolic 5'-Nucleotidase Ii Cytosolic Purine 5'-Nucleotidase 17 2.3 Yes Glycerol CSA • PDB • PDBSum
2XJE Crystal Structure Of The D52N Variant Of Cytosolic 5'-Nucleotidase Ii In Complex With Uridine 5'-Monophosphate And Adenosine Triphosphate Cytosolic Purine 5'-Nucleotidase 17 2.3 Yes Uridine-5'-Monophosphate
(3 more ⇓) 		CSA • PDB • PDBSum
2XJF Crystal Structure Of The D52N Variant Of Cytosolic 5'-Nucleotidase Ii With A Covalently Modified Asn52 Cytosolic Purine 5'-Nucleotidase 17 2.1 Yes O-Carboxy-4-Imino-L-Homoserine
(2 more ⇓) 		CSA • PDB • PDBSum
2JCM Crystal Structure Of Human Cytosolic 5'-Nucleotidase Ii In Complex With Beryllium Trifluoride Cytosolic Purine 5'-Nucleotidase 17 2.15 Aspartate Beryllium Trifluoride
(3 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Aug. 1, 2014, 12:40 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.