GLYAT_BOVIN
ID GLYAT_BOVIN Reviewed; 295 AA.
AC Q2KIR7; O46686;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Glycine N-acyltransferase {ECO:0000303|PubMed:22071172};
DE EC=2.3.1.13 {ECO:0000269|PubMed:1445276, ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678};
DE AltName: Full=Acyl-CoA:glycine N-acyltransferase;
DE Short=AAc;
DE AltName: Full=Aralkyl acyl-CoA N-acyltransferase {ECO:0000303|PubMed:1445276};
DE AltName: Full=Aralkyl acyl-CoA:amino acid N-acyltransferase {ECO:0000303|PubMed:9110242};
DE AltName: Full=Benzoyl-coenzyme A:glycine N-acyltransferase {ECO:0000303|PubMed:457678};
DE AltName: Full=Glycine N-benzoyltransferase;
DE EC=2.3.1.71 {ECO:0000269|PubMed:1445276, ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678};
GN Name=GLYAT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9110242;
RX DOI=10.1002/(sici)1522-7146(1996)11:5<211::aid-jbt1>3.0.co;2-n;
RA Vessey D.A., Lau E.;
RT "Determination of the sequence of the aralkyl acyl-CoA:amino acid N-
RT acyltransferase from bovine liver mitochondria.";
RL J. Biochem. Toxicol. 11:211-215(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-15 AND 64-89, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Liver;
RX PubMed=1445276; DOI=10.1042/bj2880315;
RA Kelley M., Vessey D.A.;
RT "Structural comparison between the mitochondrial aralkyl-CoA and
RT arylacetyl-CoA N-acyltransferases.";
RL Biochem. J. 288:315-317(1992).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=457678; DOI=10.1016/s0021-9258(18)50309-4;
RA Nandi D.L., Lucas S.V., Webster L.T. Jr.;
RT "Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme
RT A:glycine N-acyltransferase from bovine liver mitochondria. Purification
RT and characterization.";
RL J. Biol. Chem. 254:7230-7237(1979).
RN [5]
RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=22071172; DOI=10.1124/dmd.111.041657;
RA Badenhorst C.P., Jooste M., van Dijk A.A.;
RT "Enzymatic characterization and elucidation of the catalytic mechanism of a
RT recombinant bovine glycine N-acyltransferase.";
RL Drug Metab. Dispos. 40:346-352(2012).
CC -!- FUNCTION: Mitochondrial acyltransferase which transfers an acyl group
CC to the N-terminus of glycine and glutamine, although much less
CC efficiently. Can conjugate a multitude of substrates to form a variety
CC of N-acylglycines, thereby detoxify xenobiotics, such as benzoic acid
CC or salicylic acid, and endogenous organic acids, such as isovaleric
CC acid. {ECO:0000269|PubMed:457678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + glycine = an N-acylglycine + CoA + H(+);
CC Xref=Rhea:RHEA:19869, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57670, ChEBI:CHEBI:58342; EC=2.3.1.13;
CC Evidence={ECO:0000269|PubMed:1445276, ECO:0000269|PubMed:22071172,
CC ECO:0000269|PubMed:457678};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + glycine = CoA + H(+) + N-benzoylglycine;
CC Xref=Rhea:RHEA:18493, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57369, ChEBI:CHEBI:606565;
CC EC=2.3.1.71; Evidence={ECO:0000269|PubMed:1445276,
CC ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:1445276,
CC ECO:0000269|PubMed:457678}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22071172, ECO:0000269|PubMed:457678}.
CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI12537.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF045032; AAC09302.1; -; mRNA.
DR EMBL; AJ223301; CAA11242.1; -; mRNA.
DR EMBL; BC112536; AAI12537.1; ALT_INIT; mRNA.
DR RefSeq; NP_803479.1; NM_177513.2.
DR AlphaFoldDB; Q2KIR7; -.
DR SMR; Q2KIR7; -.
DR STRING; 9913.ENSBTAP00000006079; -.
DR PaxDb; Q2KIR7; -.
DR PeptideAtlas; Q2KIR7; -.
DR GeneID; 281787; -.
DR KEGG; bta:281787; -.
DR CTD; 10249; -.
DR eggNOG; ENOG502SDQB; Eukaryota.
DR InParanoid; Q2KIR7; -.
DR OrthoDB; 1221333at2759; -.
DR BRENDA; 2.3.1.13; 908.
DR BRENDA; 2.3.1.71; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0047961; F:glycine N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0047962; F:glycine N-benzoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006544; P:glycine metabolic process; IDA:UniProtKB.
DR GO; GO:0032787; P:monocarboxylic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR010313; Glycine_N-acyltransferase.
DR InterPro; IPR013652; Glycine_N-acyltransferase_C.
DR InterPro; IPR015938; Glycine_N-acyltransferase_N.
DR PANTHER; PTHR15298; PTHR15298; 1.
DR Pfam; PF08444; Gly_acyl_tr_C; 1.
DR Pfam; PF06021; Gly_acyl_tr_N; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Detoxification; Direct protein sequencing;
KW Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..295
FT /note="Glycine N-acyltransferase"
FT /id="PRO_0000281868"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 15
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 126
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 126
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 140
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 140
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 168
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 255
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 255
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT CONFLICT 85
FT /note="C -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="T -> P (in Ref. 1; AAC09302/CAA11242)"
FT /evidence="ECO:0000305"
SQ 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
