ID A0A093IVE5_FULGA Unreviewed; 566 AA.
AC A0A093IVE5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000256|ARBA:ARBA00040391};
DE EC=2.7.1.77 {ECO:0000256|ARBA:ARBA00038866};
DE EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
DE EC=3.1.3.99 {ECO:0000256|ARBA:ARBA00012894};
DE AltName: Full=Cytosolic nucleoside phosphotransferase 5'N {ECO:0000256|ARBA:ARBA00042328};
DE Flags: Fragment;
GN ORFNames=N327_05128 {ECO:0000313|EMBL:KFW05618.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW05618.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW05618.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW05618.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + inosine = adenosine + IMP; Xref=Rhea:RHEA:69596,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00036349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP + inosine = cytidine + IMP; Xref=Rhea:RHEA:69592,
CC ChEBI:CHEBI:17562, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00036204};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00036695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715;
CC Evidence={ECO:0000256|ARBA:ARBA00036695};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GMP + inosine = guanosine + IMP; Xref=Rhea:RHEA:69584,
CC ChEBI:CHEBI:16750, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00036089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053; EC=3.1.3.99;
CC Evidence={ECO:0000256|ARBA:ARBA00036953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719;
CC Evidence={ECO:0000256|ARBA:ARBA00036953};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + XMP = phosphate + xanthosine; Xref=Rhea:RHEA:28530,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18107, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57464; Evidence={ECO:0000256|ARBA:ARBA00036213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531;
CC Evidence={ECO:0000256|ARBA:ARBA00036213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a
CC 2'-deoxyribonucleoside 5'-phosphate + a ribonucleoside;
CC Xref=Rhea:RHEA:19961, ChEBI:CHEBI:18254, ChEBI:CHEBI:18274,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:65317; EC=2.7.1.77;
CC Evidence={ECO:0000256|ARBA:ARBA00036260};
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 Evidence={ECO:0000256|ARBA:ARBA00035871};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485;
CC Evidence={ECO:0000256|ARBA:ARBA00035871};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate;
CC Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57673;
CC Evidence={ECO:0000256|ARBA:ARBA00036911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380;
CC Evidence={ECO:0000256|ARBA:ARBA00036911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGMP + inosine = 2'-deoxyguanosine + IMP;
CC Xref=Rhea:RHEA:69580, ChEBI:CHEBI:17172, ChEBI:CHEBI:17596,
CC ChEBI:CHEBI:57673, ChEBI:CHEBI:58053;
CC Evidence={ECO:0000256|ARBA:ARBA00036593};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dIMP + H2O = 2'-deoxyinosine + phosphate;
CC Xref=Rhea:RHEA:29383, ChEBI:CHEBI:15377, ChEBI:CHEBI:28997,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61194;
CC Evidence={ECO:0000256|ARBA:ARBA00036191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29384;
CC Evidence={ECO:0000256|ARBA:ARBA00036191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dIMP + inosine = 2'-deoxyinosine + IMP; Xref=Rhea:RHEA:69572,
CC ChEBI:CHEBI:17596, ChEBI:CHEBI:28997, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:61194; Evidence={ECO:0000256|ARBA:ARBA00036258};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine + UMP = IMP + uridine; Xref=Rhea:RHEA:69588,
CC ChEBI:CHEBI:16704, ChEBI:CHEBI:17596, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:58053; Evidence={ECO:0000256|ARBA:ARBA00036826};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR017434-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000256|ARBA:ARBA00009589}.
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DR EMBL; KK600173; KFW05618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093IVE5; -.
DR Proteomes; UP000053806; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046037; P:GMP metabolic process; IEA:UniProt.
DR CDD; cd07522; HAD_cN-II; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016695; Pur_nucleotidase.
DR NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR12103:SF17; CYTOSOLIC PURINE 5'-NUCLEOTIDASE; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017434-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR017434-2};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053806};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 494..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT BINDING 54
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT NON_TER 566
FT /evidence="ECO:0000313|EMBL:KFW05618.1"
SQ SEQUENCE 566 AA; 65537 MW; 2625879CB6C05AA5 CRC64;
MTTSWSDRLQ NAADLPANMD GHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
KSPEYESLGF DLTVERLVSI GYPHELLNFV YDPAFPTRGL VFDTHYGNLL KVDAYGNLLV
CAHGFNFLRG PETRDQYPNK FIQRDDTDRF YILNTLFNLP ETYLLACLVD FFTNCDRYTS
CETGFKDGDL FMSFRSMFQD VRDAVDWVHY KGSLKEKTLE NLEKYVVKDG KLPLLLSRMN
EVGKVFLVTN SDYKYTDKIM TYLFDFPHGP KPGSAHRPWQ SYFDLILVDA RKPLFFGEGT
VLRQVDTVTG KLKIGTYTGP LQHGIVYSGG SSDTVCDLLG AKGKDILYIG DHIFGDILKS
KKRQGWRTFL VIPELAQELH VWTDKSALFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA
HVLMPHESTV EHTHVDINEK ESPMATRNRT SVDFKDSDYK RHQLTRSISE IKPPNLFPQA
PQEITHCHDE DDDEEEEEEE EEEEEE
//
