ID   HINT3_PONAB             Reviewed;         182 AA.
AC   Q5R9L4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Adenosine 5'-monophosphoramidase HINT3 {ECO:0000250|UniProtKB:Q9NQE9};
DE            EC=3.9.1.- {ECO:0000250|UniProtKB:Q9NQE9};
DE   AltName: Full=Histidine triad nucleotide-binding protein 3;
GN   Name=HINT3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exhibits adenosine 5'-monophosphoramidase activity,
CC       hydrolyzing purine nucleotide phosphoramidates with a single phosphate
CC       group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP
CC       and NH2 (By similarity). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-
CC       acetyl lysine methyl ester)) generated by lysine tRNA ligase (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NQE9}.
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:Q9NQE9};
CC   -!- SUBUNIT: Forms dimers to octamers and even larger oligomer (By
CC       similarity). Interacts with CALM1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9CPS6, ECO:0000250|UniProtKB:Q9NQE9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQE9}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9NQE9}.
CC   -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR   EMBL; CR859092; CAH91284.1; -; mRNA.
DR   EMBL; CR859373; CAH91546.1; -; mRNA.
DR   RefSeq; NP_001125760.1; NM_001132288.2.
DR   AlphaFoldDB; Q5R9L4; -.
DR   SMR; Q5R9L4; -.
DR   STRING; 9601.ENSPPYP00000019023; -.
DR   Ensembl; ENSPPYT00000019774; ENSPPYP00000019023; ENSPPYG00000016989.
DR   GeneID; 100172685; -.
DR   KEGG; pon:100172685; -.
DR   CTD; 135114; -.
DR   eggNOG; KOG4359; Eukaryota.
DR   GeneTree; ENSGT00510000047616; -.
DR   HOGENOM; CLU_056776_4_2_1; -.
DR   InParanoid; Q5R9L4; -.
DR   OMA; CRIAGRQ; -.
DR   OrthoDB; 1496385at2759; -.
DR   TreeFam; TF353069; -.
DR   Proteomes; UP000001595; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.428.10; -; 1.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   SUPFAM; SSF54197; SSF54197; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT   CHAIN           2..182
FT                   /note="Adenosine 5'-monophosphoramidase HINT3"
FT                   /id="PRO_0000324330"
FT   DOMAIN          49..160
FT                   /note="HIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT   MOTIF           143..147
FT                   /note="Histidine triad motif"
FT   ACT_SITE        145
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT   BINDING         76..77
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P49773"
FT   BINDING         145..147
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P49773"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQE9"
SQ   SEQUENCE   182 AA;  20268 MW;  096690FA5582B319 CRC64;
     MAEEQVNLSA GLAPDCEASA TAESTVSLVG TCEAAAKSPE PKDSDSTCVF CRIAGRQDPG
     TELLHCENED LICFKDIKPA ATHHYLVVPK KHIGNCRTLR KDQVELVENM VTVGKTILER
     NNFTDFTNVR MGFHMPPFCS ISHLHLHVLA PVDQLGFLSK LVYRVNSYWF ITADHLIEKL
     RT