ID   HISAT_SCOAU             Reviewed;         337 AA.
AC   U3U715;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Histidine N-acetyltransferase;
DE            EC=2.3.1.33 {ECO:0000269|PubMed:24121108};
DE   Flags: Precursor;
GN   Name=hisat;
OS   Scomber australasicus (Blue mackerel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Scomber.
OX   NCBI_TaxID=29150;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-22 AND 52-61, FUNCTION,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CATALYTIC ACTIVITY.
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).
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   -!- 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; AB777506; BAO00799.1; -; mRNA.
DR   EMBL; AB777507; BAO00800.1; -; mRNA.
DR   AlphaFoldDB; U3U715; -.
DR   SMR; U3U715; -.
DR   BRENDA; 2.3.1.33; 5630.
DR   GO; GO:0047981; F:histidine N-acetyltransferase activity; ISS: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; Direct protein sequencing; Transferase.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:24121108"
FT                   /id="PRO_0000432394"
FT   CHAIN           3..337
FT                   /note="Histidine N-acetyltransferase"
FT                   /id="PRO_0000432395"
FT   DOMAIN          21..156
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   337 AA;  38228 MW;  F34E1C2E225F43E6 CRC64;
     MKIDTSLTMP QLPEALSQAG LQFAVATEED FDEIMAMSQD IYGGLDYLPT RYTSWLQETN
     RTVILARKQG KVIALESVCV IDNGETMLVE GLRVAPQERG KGVAGVLLRF CCELVKSKYP
     EVKVTRLTRD DQLGPKDFQK YRLITKQGIL LVRFRAEDLK LRLSELNLGG DIQSSLSTSS
     SNTPPVRLDH TAIHRLYLTT DLMQGVLPNA TIIQDWQPFK PLPSNMAILL KKDIDWMVDD
     VANPTMASLC TFPYRVPVGD DWYYLNIDMF GKDLDLAQQQ FLCHLQRHTT TLKGHVMCQM
     FLDPPLWKPM AEFCNKTLSV ELVKEYTEQC VVESDVV