ID   HISAT_ORENI             Reviewed;         337 AA.
AC   I3J7Q8;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Histidine N-acetyltransferase;
DE            EC=2.3.1.33 {ECO:0000269|PubMed:24121108};
DE   Flags: Precursor;
GN   Name=hisat;
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC
RP   ACTIVITY, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=24121108; DOI=10.1016/j.bbagen.2013.10.004;
RA   Yamada S., Arikawa S.;
RT   "An ectotherm homologue of human predicted gene NAT16 encodes histidine N-
RT   acetyltransferase responsible for Nalpha-acetylhistidine synthesis.";
RL   Biochim. Biophys. Acta 1840:434-442(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The genome sequence of oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=7492584; DOI=10.1016/0304-4165(95)00089-t;
RA   Yamada S., Tanaka Y., Furuichi M.;
RT   "Partial purification and characterization of histidine acetyltransferase
RT   in brain of Nile tilapia (Oreochromis niloticus).";
RL   Biochim. Biophys. Acta 1245:239-247(1995).
CC   -!- FUNCTION: Enzyme responsible for the N-acetyl-histidine (NAH)
CC       synthesis, which is a major constituent of brain and lens of
CC       ectothermic vertebrates. {ECO:0000269|PubMed:24121108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-histidine = CoA + H(+) + N(alpha)-acetyl-L-
CC         histidine; Xref=Rhea:RHEA:24596, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:57772; EC=2.3.1.33;
CC         Evidence={ECO:0000269|PubMed:24121108};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27 uM for acetyl-CoA {ECO:0000269|PubMed:7492584};
CC         KM=450 uM for L-histidine {ECO:0000269|PubMed:7492584};
CC       pH dependence:
CC         Optimum pH is 7.0-9.5. {ECO:0000269|PubMed:7492584};
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in the brain and lens.
CC       {ECO:0000269|PubMed:24121108}.
CC   -!- MISCELLANEOUS: Strong histidine N-acetyltransferase activity has been
CC       detected in ectothermic vertebrates and not in endothermic birds and
CC       mammals. {ECO:0000305|PubMed:24121108}.
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DR   EMBL; AB701381; BAO00797.1; -; mRNA.
DR   EMBL; AB701382; BAO00798.1; -; mRNA.
DR   EMBL; AERX01050570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AERX01050571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AERX01050572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AERX01050573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001272326.1; NM_001285397.1.
DR   RefSeq; XP_005463482.1; XM_005463425.3.
DR   RefSeq; XP_019202559.1; XM_019347014.1.
DR   AlphaFoldDB; I3J7Q8; -.
DR   SMR; I3J7Q8; -.
DR   STRING; 8128.ENSONIP00000004898; -.
DR   Ensembl; ENSONIT00000004901; ENSONIP00000004898; ENSONIG00000003888.
DR   GeneID; 100702495; -.
DR   KEGG; onl:100702495; -.
DR   CTD; 375607; -.
DR   eggNOG; ENOG502QW73; Eukaryota.
DR   GeneTree; ENSGT00390000016398; -.
DR   HOGENOM; CLU_074598_0_0_1; -.
DR   InParanoid; I3J7Q8; -.
DR   OMA; SWLQETN; -.
DR   OrthoDB; 1293735at2759; -.
DR   TreeFam; TF331490; -.
DR   BRENDA; 2.3.1.33; 4429.
DR   Proteomes; UP000005207; Linkage group LG3.
DR   GO; GO:0047981; F:histidine N-acetyltransferase activity; IDA:UniProtKB.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:U3U715"
FT                   /id="PRO_0000432392"
FT   CHAIN           3..337
FT                   /note="Histidine N-acetyltransferase"
FT                   /id="PRO_0000432393"
FT   DOMAIN          21..157
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   337 AA;  38413 MW;  57A8C0FACAA416AC CRC64;
     MKIDTSLNMP QLPEALSQAG LQFSVATEED FDEIMAMSQD IYGGLDYLPT RYTSWLQDTN
     RTVILARKHG KVIALESVCV IDDGETMLVE GLRVAPQERG KGVAGVLLRF CAELVKSRYP
     EVKVCRLTRD DQLGPKDFEK YRIITKQGIL LMRFRAEDLK LHLSEFGLEG DNESTLSTFC
     SSPPPVRLDH TAIQQLYLNS DLLHGVLPNA TIIQDWQPFK LLPSNMAILL KKEIDWMVDD
     MSNPTVASLC TFPFRVPIGD DWYYLNIDMF GKDLALARQQ FLYHLQRHTA TLKGHVMCQM
     FLDPPLWKAM AEFCHNTLSV ELVKEYTEQC VVECDLI