ID   A0A087V7Q7_BALRE        Unreviewed;       635 AA.
AC   A0A087V7Q7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Choline O-acetyltransferase {ECO:0000256|ARBA:ARBA00040495};
DE            EC=2.3.1.6 {ECO:0000256|ARBA:ARBA00039091};
DE   Flags: Fragment;
GN   ORFNames=N312_13247 {ECO:0000313|EMBL:KFO08649.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO08649.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO08649.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO08649.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh)
CC       from acetyl CoA and choline at cholinergic synapses.
CC       {ECO:0000256|ARBA:ARBA00037088}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + choline = acetylcholine + CoA;
CC         Xref=Rhea:RHEA:18821, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036720};
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; KL483032; KFO08649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087V7Q7; -.
DR   Proteomes; UP000053309; Unassembled WGS sequence.
DR   GO; GO:0004102; F:choline O-acetyltransferase activity; ISS:AgBase.
DR   GO; GO:0060416; P:response to growth hormone; ISS:AgBase.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF14; CHOLINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003801};
KW   Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          22..601
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        330
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO08649.1"
FT   NON_TER         635
FT                   /evidence="ECO:0000313|EMBL:KFO08649.1"
SQ   SEQUENCE   635 AA;  72259 MW;  A9C5E5411BC8CCDD CRC64;
     EKNMQKKEKD TCSKDETAVP KLPVPPLQQT LGMYLKCTKH LVPEEQFRKT KVIVEQFGIA
     GGLGETLQQI LEERREKTTN WVFNYWLDDM YLNNRLALPV NSSPAIIFAR QYFKDVNDQL
     RFAANLISGV QDYKALLDTH ALPVDFARGQ LSGHPLCMKQ YYGLFSSYRL PGHTKDTLVA
     QKSSVMPEPE HIIVACNNQF FVLDVVINFR RLSEGDLFTQ LRKIAKMAEN EEEMLPPIGL
     LTTDGRTEWA EARTILMKDS TNRDSLDMIE RCICLVCLDS PSGVELNDTN MALQLLHGGG
     YHKNGANRWY DKPMQFVVGR DGVCGTVCEH SPFDGIVLVQ CTEHLLKHMK ESSKKLVRAD
     SVSELPAPRR LRWKCSPEIQ AHLASSSEKL QRIVKNLDFI AYKFENYGKE FIKKQKISPD
     AYIQVALQLA FYRCHRRLVP TYESASIRRF DEGRVDNIRS ATLEAFAFVK AMTDDKTALS
     ESEKMQRFKD AIAAQTNYTI LAITGMAIDN HLLGLREVAR EHFKELPEIF TDETYLTSNR
     FILSTSQVPT TMEMFCCYGP VVPNGYGACY NPQPEHILFC ISSFKDCKET SSDMFAKAVE
     ESLLDMRDLC SKCNSTMAKP LAKQEADTQP QSDRK
//