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Glycine N-acyltransferase (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase) (AAc) (Aralkyl acyl-CoA N-acyltransferase) (Aralkyl acyl-CoA:amino acid N-acyltransferase) (Benzoyl-coenzyme A:glycine N-acyltransferase) (Glycine N-benzoyltransferase) (EC 2.3.1.71)

 GLYAT_BOVIN             Reviewed;         295 AA.
Q2KIR7; O46686;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
05-DEC-2018, entry version 64.
RecName: Full=Glycine N-acyltransferase {ECO:0000303|PubMed:22071172};
EC=2.3.1.13 {ECO:0000269|PubMed:1445276, ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678};
AltName: Full=Acyl-CoA:glycine N-acyltransferase;
Short=AAc;
AltName: Full=Aralkyl acyl-CoA N-acyltransferase {ECO:0000303|PubMed:1445276};
AltName: Full=Aralkyl acyl-CoA:amino acid N-acyltransferase {ECO:0000303|PubMed:9110242};
AltName: Full=Benzoyl-coenzyme A:glycine N-acyltransferase {ECO:0000303|PubMed:457678};
AltName: Full=Glycine N-benzoyltransferase;
EC=2.3.1.71 {ECO:0000269|PubMed:1445276, ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678};
Name=GLYAT;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9110242;
DOI=10.1002/(SICI)1522-7146(1996)11:5<211::AID-JBT1>3.0.CO;2-N;
Vessey D.A., Lau E.;
"Determination of the sequence of the aralkyl acyl-CoA:amino acid N-
acyltransferase from bovine liver mitochondria.";
J. Biochem. Toxicol. 11:211-215(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Testis;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 1-15 AND 64-89, CATALYTIC ACTIVITY, AND
SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=1445276; DOI=10.1042/bj2880315;
Kelley M., Vessey D.A.;
"Structural comparison between the mitochondrial aralkyl-CoA and
arylacetyl-CoA N-acyltransferases.";
Biochem. J. 288:315-317(1992).
[4]
CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=457678;
Nandi D.L., Lucas S.V., Webster L.T. Jr.;
"Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-
coenzyme A:glycine N-acyltransferase from bovine liver mitochondria.
Purification and characterization.";
J. Biol. Chem. 254:7230-7237(1979).
[5]
CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=22071172; DOI=10.1124/dmd.111.041657;
Badenhorst C.P., Jooste M., van Dijk A.A.;
"Enzymatic characterization and elucidation of the catalytic mechanism
of a recombinant bovine glycine N-acyltransferase.";
Drug Metab. Dispos. 40:346-352(2012).
-!- FUNCTION: Mitochondrial acyltransferase which transfers an acyl
group to the N-terminus of glycine and glutamine, although much
less efficiently. Can conjugate a multitude of substrates to form
a variety of N-acylglycines, thereby detoxify xenobiotics, such as
benzoic acid or salicylic acid, and endogenous organic acids, such
as isovaleric acid. {ECO:0000269|PubMed:457678}.
-!- CATALYTIC ACTIVITY:
Reaction=an acyl-CoA + glycine = an N-acylglycine + CoA + H(+);
Xref=Rhea:RHEA:19869, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57305, ChEBI:CHEBI:57670, ChEBI:CHEBI:58342;
EC=2.3.1.13; Evidence={ECO:0000269|PubMed:1445276,
ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678};
-!- CATALYTIC ACTIVITY:
Reaction=benzoyl-CoA + glycine = CoA + H(+) + N-benzoylglycine;
Xref=Rhea:RHEA:18493, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57305, ChEBI:CHEBI:57369, ChEBI:CHEBI:606565;
EC=2.3.1.71; Evidence={ECO:0000269|PubMed:1445276,
ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678};
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:1445276,
ECO:0000269|PubMed:457678}.
-!- TISSUE SPECIFICITY: Detected in liver (at protein level).
{ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678}.
-!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI12537.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF045032; AAC09302.1; -; mRNA.
EMBL; AJ223301; CAA11242.1; -; mRNA.
EMBL; BC112536; AAI12537.1; ALT_INIT; mRNA.
RefSeq; NP_803479.1; NM_177513.2.
UniGene; Bt.62101; -.
SMR; Q2KIR7; -.
STRING; 9913.ENSBTAP00000006079; -.
PaxDb; Q2KIR7; -.
PeptideAtlas; Q2KIR7; -.
PRIDE; Q2KIR7; -.
GeneID; 281787; -.
KEGG; bta:281787; -.
CTD; 10249; -.
eggNOG; ENOG410IJUM; Eukaryota.
eggNOG; ENOG4111428; LUCA.
HOGENOM; HOG000263599; -.
HOVERGEN; HBG107953; -.
InParanoid; Q2KIR7; -.
KO; K00628; -.
BRENDA; 2.3.1.13; 908.
BRENDA; 2.3.1.71; 908.
Proteomes; UP000009136; Unplaced.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0047961; F:glycine N-acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0047962; F:glycine N-benzoyltransferase activity; IDA:UniProtKB.
GO; GO:0006544; P:glycine metabolic process; IDA:UniProtKB.
GO; GO:0032787; P:monocarboxylic acid metabolic process; IDA:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR010313; Glycine_N-acyltransferase.
InterPro; IPR013652; Glycine_N-acyltransferase_C.
InterPro; IPR015938; Glycine_N-acyltransferase_N.
PANTHER; PTHR15298; PTHR15298; 1.
Pfam; PF08444; Gly_acyl_tr_C; 1.
Pfam; PF06021; Gly_acyl_tr_N; 1.
SUPFAM; SSF55729; SSF55729; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Complete proteome; Detoxification;
Direct protein sequencing; Mitochondrion; Reference proteome;
Transferase.
CHAIN 1 295 Glycine N-acyltransferase.
/FTId=PRO_0000281868.
MOD_RES 15 15 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 15 15 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 126 126 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 126 126 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 140 140 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 140 140 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 158 158 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 168 168 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 255 255 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 255 255 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
CONFLICT 85 85 C -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 211 211 T -> P (in Ref. 1; AAC09302/CAA11242).
{ECO:0000305}.
SEQUENCE 295 AA; 33907 MW; 2930A90A95623806 CRC64;
MFLLQGAQML QMLEKSLRKS LPMSLKVYGT VMHMNHGNPF NLKALVDKWP DFQTVVIRPQ
EQDMKDDLDH YTNTYHVYSE DLKNCQEFLD LPEVINWKQH LQIQSTQSSL NEVIQNLAAT
KSFKVKRSKN ILYMASETIK ELTPSLLDVK NLPVGDGKPK AIDPEMFKLS SVDPSHAAVV
NRFWLFGGNE RSLRFIERCI QSFPNFCLLG TEGTPVSWSL MDQTGEMRMA GTLPEYRAQG
LVTHAIYQQA QCLLKRGFPV YSHVDPKNQI MQKMSQSLNH VPMPSDWNQW NCEPL


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