HINT_HAEIN
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 03-AUG-2022, entry version 109.
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; Proteobacteria; 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};
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DR EMBL; L42023; AAC22621.1; ALT_INIT; Genomic_DNA.
DR PIR; G64162; G64162.
DR RefSeq; NP_439122.2; NC_000907.1.
DR RefSeq; WP_005627389.1; 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 PhylomeDB; P44956; -.
DR BioCyc; HINF71421:G1GJ1-1002-MON; -.
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:0016787; F:hydrolase 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 Gene3D; 3.30.428.10; -; 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; PTHR23089; 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 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
