ID A0A2I3M8B9_PAPAN Unreviewed; 561 AA.
AC A0A2I3M8B9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 29.
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};
GN Name=NT5C2 {ECO:0000313|Ensembl:ENSPANP00000031904.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000031904.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000031904.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000031904.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_003904252.1; XM_003904203.3.
DR AlphaFoldDB; A0A2I3M8B9; -.
DR SMR; A0A2I3M8B9; -.
DR Ensembl; ENSPANT00000049643.2; ENSPANP00000031904.2; ENSPANG00000020954.3.
DR GeneID; 101000292; -.
DR KEGG; panu:101000292; -.
DR CTD; 22978; -.
DR GeneTree; ENSGT00940000162369; -.
DR Proteomes; UP000028761; Chromosome 11.
DR Bgee; ENSPANG00000020954; Expressed in thymus and 67 other cell types or tissues.
DR ExpressionAtlas; A0A2I3M8B9; baseline.
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:UP000028761};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 538..561
FT /note="Disordered"
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"
SQ SEQUENCE 561 AA; 64970 MW; 4C27D762575E0EA2 CRC64;
MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS
CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA
HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA
PQEITHCHDE DDDEEEEEEE E
//
