ID   HINT_HAEIN              Reviewed;         116 AA.
AC   P44956;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Purine nucleoside phosphoramidase {ECO:0000250|UniProtKB:P0ACE7};
DE            EC=3.9.1.- {ECO:0000250|UniProtKB:P0ACE7};
DE   AltName: Full=Histidine triad nucleotide binding protein HI_0961;
DE            Short=HIT protein;
GN   OrderedLocusNames=HI_0961;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
CC   -!- FUNCTION: Hydrolyzes purine nucleotide phosphoramidates, including
CC       adenosine 5'monophosphoramidate (AMP-NH2), adenosine
CC       5'monophosphomorpholidate (AMP-morpholidate), guanosine
CC       5'monophosphomorpholidate (GMP-morpholidate) and tryptamine 5'guanosine
CC       monophosphate (TpGd). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-
CC       acetyl lysine methyl ester)) generated by lysine tRNA ligase and lysyl-
CC       GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)).
CC       {ECO:0000250|UniProtKB:P0ACE7}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0ACE7}.
CC   -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22621.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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   EMBL; L42023; AAC22621.1; ALT_INIT; Genomic_DNA.
DR   PIR; G64162; G64162.
DR   RefSeq; NP_439122.2; NC_000907.1.
DR   AlphaFoldDB; P44956; -.
DR   SMR; P44956; -.
DR   STRING; 71421.HI_0961; -.
DR   EnsemblBacteria; AAC22621; AAC22621; HI_0961.
DR   KEGG; hin:HI_0961; -.
DR   PATRIC; fig|71421.8.peg.1003; -.
DR   eggNOG; COG0537; Bacteria.
DR   HOGENOM; CLU_056776_8_1_6; -.
DR   OrthoDB; 9784774at2; -.
DR   PhylomeDB; P44956; -.
DR   BioCyc; HINF71421:G1GJ1-1002-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0055130; P:D-alanine catabolic process; IBA:GO_Central.
DR   CDD; cd01276; PKCI_related; 1.
DR   Gene3D; 3.30.428.10; HIT-like; 1.
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; PTHR23089; HISTIDINE TRIAD HIT PROTEIN; 1.
DR   PANTHER; PTHR23089:SF51; PURINE NUCLEOSIDE PHOSPHORAMIDASE; 1.
DR   Pfam; PF01230; HIT; 1.
DR   PRINTS; PR00332; HISTRIAD.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..116
FT                   /note="Purine nucleoside phosphoramidase"
FT                   /id="PRO_0000109833"
FT   DOMAIN          6..115
FT                   /note="HIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT   MOTIF           99..105
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   ACT_SITE        101
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   BINDING         30..32
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   BINDING         88
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   BINDING         96..97
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
FT   BINDING         101..103
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACE7"
SQ   SEQUENCE   116 AA;  12887 MW;  904B9A3211757F12 CRC64;
     MAEETIFSKI IRKEIPANIV YQDELVTAFR DISPQAKTHI LIIPNKVIPT VNDVTEQDEV
     ALGRLFSVAA KLAKEEGVAE DGYRLIVNCN KHGGQEVFHL HMHLVGGEPL GRMLAK
//