HNT1_SCHPO
ID HNT1_SCHPO Reviewed; 133 AA.
AC O94586;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Adenosine 5'-monophosphoramidase hnt1 {ECO:0000250|UniProtKB:P49773};
DE EC=3.-.-.- {ECO:0000250|UniProtKB:P49773};
DE AltName: Full=Histidine triad nucleotide-binding protein HNT1 {ECO:0000250|UniProtKB:P49773};
DE Short=HINT {ECO:0000250|UniProtKB:P49773};
DE AltName: Full=Hit family protein 1 {ECO:0000250|UniProtKB:P49773};
GN Name=hnt1; ORFNames=SPCC1442.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Hydrolyzes adenosine 5'-monophosphoramidate substrates such
CC as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl
CC lysine methyl ester and AMP-NH2. {ECO:0000250|UniProtKB:P49773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+);
CC Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57890, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P49773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67917;
CC Evidence={ECO:0000250|UniProtKB:P49773};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q04344};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q59WG0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21448.1; -; Genomic_DNA.
DR PIR; T40979; T40979.
DR RefSeq; NP_588328.1; NM_001023319.2.
DR AlphaFoldDB; O94586; -.
DR SMR; O94586; -.
DR BioGRID; 275405; 13.
DR STRING; 4896.SPCC1442.14c.1; -.
DR MaxQB; O94586; -.
DR PaxDb; O94586; -.
DR EnsemblFungi; SPCC1442.14c.1; SPCC1442.14c.1:pep; SPCC1442.14c.
DR GeneID; 2538824; -.
DR KEGG; spo:SPCC1442.14c; -.
DR PomBase; SPCC1442.14c; hnt1.
DR VEuPathDB; FungiDB:SPCC1442.14c; -.
DR eggNOG; KOG3275; Eukaryota.
DR HOGENOM; CLU_056776_3_0_1; -.
DR InParanoid; O94586; -.
DR OMA; SDCLFCK; -.
DR PhylomeDB; O94586; -.
DR PRO; PR:O94586; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; ISO:PomBase.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; ISO:PomBase.
DR CDD; cd01277; HINT_subgroup; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR039384; HINT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR46648; PTHR46648; 1.
DR Pfam; PF01230; HIT; 1.
DR PRINTS; PR00332; HISTRIAD.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..133
FT /note="Adenosine 5'-monophosphoramidase hnt1"
FT /id="PRO_0000314651"
FT DOMAIN 4..107
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 92..96
FT /note="Histidine triad motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ACT_SITE 94
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 29..30
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 81
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 87..89
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 94..96
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
SQ SEQUENCE 133 AA; 14580 MW; E85969D74343A6B6 CRC64;
MSCIFCKIVK GDIPCVKLAE TALSLAFLDI APTSKGHALV IPKEHAAKMH ELSDESCADI
LPLVKKVTKA IGPENYNVLQ NNGRIAHQFV DHVHFHIIPK PNEEYGLGVG WPSYPISPEE
IKALGEEISS KIK
