HIT_ENTHI
ID HIT_ENTHI Reviewed; 113 AA.
AC C4LYI2;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Histidine triad nucleotide-binding protein;
DE EC=3.-.-.-;
GN ORFNames=EHI_093910;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=15729342; DOI=10.1038/nature03291;
RA Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA Barrell B.G., Fraser C.M., Hall N.;
RT "The genome of the protist parasite Entamoeba histolytica.";
RL Nature 433:865-868(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEXES WITH AMP AND GMP.
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of a histidine triad family protein from Entamoeba
RT histolytica, bound to sulfate.";
RL Submitted (MAY-2011) to the PDB data bank.
CC -!- FUNCTION: Hydrolyzes purine nucleotide phosphoramidates with a single
CC phosphate group, including adenosine 5'monophosphoramidate (AMP-NH2),
CC adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine
CC 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP
CC (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by
CC lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP
CC (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine
CC methyl ester. May also function as scaffolding protein that mediates
CC protein-protein interactions (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR EMBL; DS571179; EAL50232.1; -; Genomic_DNA.
DR RefSeq; XP_655618.1; XM_650526.1.
DR PDB; 3OJ7; X-ray; 1.40 A; A=1-113.
DR PDB; 3OMF; X-ray; 1.80 A; A=1-113.
DR PDB; 3OXK; X-ray; 1.55 A; A=1-113.
DR PDBsum; 3OJ7; -.
DR PDBsum; 3OMF; -.
DR PDBsum; 3OXK; -.
DR AlphaFoldDB; C4LYI2; -.
DR SMR; C4LYI2; -.
DR STRING; 5759.rna_EHI_093910-1; -.
DR EnsemblProtists; rna_EHI_093910-1; rna_EHI_093910-1; EHI_093910.
DR GeneID; 3409936; -.
DR KEGG; ehi:EHI_093910; -.
DR VEuPathDB; AmoebaDB:EHI5A_161370; -.
DR VEuPathDB; AmoebaDB:EHI7A_185610; -.
DR VEuPathDB; AmoebaDB:EHI8A_215710; -.
DR VEuPathDB; AmoebaDB:EHI_093910; -.
DR VEuPathDB; AmoebaDB:KM1_210220; -.
DR eggNOG; KOG3275; Eukaryota.
DR HOGENOM; CLU_056776_8_1_1; -.
DR InParanoid; C4LYI2; -.
DR OMA; SDCLFCK; -.
DR EvolutionaryTrace; C4LYI2; -.
DR Proteomes; UP000001926; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 3D-structure; Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..113
FT /note="Histidine triad nucleotide-binding protein"
FT /id="PRO_0000421976"
FT DOMAIN 6..113
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 97..101
FT /note="Histidine triad motif"
FT ACT_SITE 99
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 31..32
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 86
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 92..94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 99..101
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT HELIX 1..4
FT /evidence="ECO:0007829|PDB:3OXK"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:3OJ7"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:3OJ7"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:3OJ7"
FT STRAND 35..46
FT /evidence="ECO:0007829|PDB:3OJ7"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3OJ7"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3OJ7"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:3OJ7"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3OJ7"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:3OJ7"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3OJ7"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3OJ7"
SQ SEQUENCE 113 AA; 12701 MW; BC13C764B502686F CRC64;
MADSCIFCKI AQKQIPSTIV YEDDEIFAFK DINPIAPIHI LVIPKQHIAS LNEITEENEA
FIGKVLYKVS LIGKKECPEG YRVVNNIGED AGQTVKHIHF HILGGKKLAW DKL
