HNT1_CANAL
ID HNT1_CANAL Reviewed; 152 AA.
AC Q59WG0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Adenosine 5'-monophosphoramidase HNT1 {ECO:0000303|PubMed:17588813};
DE EC=3.-.-.- {ECO:0000305|PubMed:17588813};
DE AltName: Full=Histidine triad nucleotide-binding protein HNT1 {ECO:0000303|PubMed:30622225};
DE Short=HINT {ECO:0000303|PubMed:30622225};
GN Name=HNT1 {ECO:0000303|PubMed:30622225}; OrderedLocusNames=orf19.2341;
GN ORFNames=CAALFM_C110780CA;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=17588813; DOI=10.1016/j.ijmm.2007.03.020;
RA Kusch H., Engelmann S., Bode R., Albrecht D., Morschhauser J., Hecker M.;
RT "A proteomic view of Candida albicans yeast cell metabolism in exponential
RT and stationary growth phases.";
RL Int. J. Med. Microbiol. 298:291-318(2008).
RN [5]
RP INDUCTION.
RX PubMed=23194472; DOI=10.1111/omi.12006;
RA Bandara H.M., Cheung B.P.K., Watt R.M., Jin L.J., Samaranayake L.P.;
RT "Pseudomonas aeruginosa lipopolysaccharide inhibits Candida albicans hyphae
RT formation and alters gene expression during biofilm development.";
RL Mol. Oral. Microbiol. 28:54-69(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS), AND SUBUNIT.
RX PubMed=30622225; DOI=10.14348/molcells.2018.0377;
RA Jung A., Yun J.S., Kim S., Kim S.R., Shin M., Cho D.H., Choi K.S.,
RA Chang J.H.;
RT "Crystal Structure of histidine triad nucleotide-binding protein from the
RT pathogenic fungus Candida albicans.";
RL Mol. Cells 42:56-66(2019).
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:0000269|PubMed:30622225}.
CC -!- INDUCTION: Expression is decreased at the stationary phase
CC (PubMed:17588813). Expression in suppressed in the presence of
CC Pseudomonas aeruginosa lipopolysaccharide (LPS) (PubMed:23194472).
CC {ECO:0000269|PubMed:17588813, ECO:0000269|PubMed:23194472}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26705.1; -; Genomic_DNA.
DR RefSeq; XP_713946.1; XM_708853.1.
DR PDB; 6IQ1; X-ray; 2.48 A; A/B/C/D=1-152.
DR PDBsum; 6IQ1; -.
DR AlphaFoldDB; Q59WG0; -.
DR SMR; Q59WG0; -.
DR STRING; 237561.Q59WG0; -.
DR EnsemblFungi; KHC83822; KHC83822; W5Q_01042.
DR EnsemblFungi; KHC89260; KHC89260; I503_01052.
DR GeneID; 3644441; -.
DR KEGG; cal:CAALFM_C110780CA; -.
DR CGD; CAL0000178567; HNT1.
DR VEuPathDB; FungiDB:C1_10780C_A; -.
DR eggNOG; KOG3275; Eukaryota.
DR HOGENOM; CLU_056776_3_0_1; -.
DR InParanoid; Q59WG0; -.
DR OMA; SDCLFCK; -.
DR OrthoDB; 1190598at2759; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; IEA:EnsemblFungi.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IBA:GO_Central.
DR GO; GO:0010043; P:response to zinc ion; IEA:EnsemblFungi.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Nucleotide-binding; Reference proteome.
FT CHAIN 1..152
FT /note="Adenosine 5'-monophosphoramidase HNT1"
FT /id="PRO_0000453884"
FT DOMAIN 8..119
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 104..108
FT /note="Histidine triad motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ACT_SITE 106
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 33..34
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 93
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 BINDING 106..108
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6IQ1"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6IQ1"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:6IQ1"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:6IQ1"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:6IQ1"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6IQ1"
FT HELIX 130..147
FT /evidence="ECO:0007829|PDB:6IQ1"
SQ SEQUENCE 152 AA; 16986 MW; CFE47D525801B5FA CRC64;
MASHASCIFC KIIKGEIPSF KLIETAKTYS FLDIQPIAEA HVLIIPKHHG AKLHNIPDDY
LSDILPVVKK LTKVLKLDEN NTPEGEGYNV LQNNGRIAHQ VVDHVHFHLI PKKDEATGLG
VGWPAEATDF DKLGKLHEKL KEELAKVDNE KL
