GLYAL_BOVIN
ID GLYAL_BOVIN Reviewed; 295 AA.
AC O77512; O62832; Q9T2T9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glycine N-phenylacetyltransferase;
DE EC=2.3.1.192;
DE AltName: Full=ArAlk;
DE AltName: Full=Arylacetyl-CoA N-acyltransferase;
DE Short=Arylacetyltransferase;
DE AltName: Full=Arylacetyl-CoA:amino acid N-acyltransferase;
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 [GENOMIC DNA / MRNA], AND PROTEIN SEQUENCE OF 229-260.
RC TISSUE=Liver;
RX PubMed=9664233;
RX DOI=10.1002/(sici)1099-0461(1998)12:5<275::aid-jbt3>3.0.co;2-i;
RA Vessey D.A., Lau E.;
RT "Determination of the sequence of the arylacetyl acyl-CoA:amino acid N-
RT acyltransferase from bovine liver mitochondria and its homology to the
RT aralkyl acyl-CoA:amino acid N-acyltransferase.";
RL J. Biochem. Mol. Toxicol. 12:275-279(1998).
RN [2]
RP PROTEIN SEQUENCE OF 64-89, CATALYTIC ACTIVITY, AND SUBCELLULAR 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).
CC -!- FUNCTION: Mitochondrial acyltransferase which transfers the acyl group
CC to the N-terminus of glycine. Can conjugate a multitude of substrates
CC to form a variety of N-acylglycines. Catalyzes the conjugation of
CC arylacetic acids with glycine but does not have activity towards any
CC alkyl-CoA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + phenylacetyl-CoA = CoA + H(+) + phenylacetylglycine;
CC Xref=Rhea:RHEA:27850, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57390, ChEBI:CHEBI:60874;
CC EC=2.3.1.192; Evidence={ECO:0000269|PubMed:1445276};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:1445276}.
CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ001396; CAA04726.1; -; Genomic_DNA.
DR EMBL; AF022073; AAC33282.1; -; mRNA.
DR PIR; S27170; S27170.
DR RefSeq; NP_803452.1; NM_177486.2.
DR RefSeq; XP_005216632.1; XM_005216575.3.
DR AlphaFoldDB; O77512; -.
DR SMR; O77512; -.
DR PaxDb; O77512; -.
DR PeptideAtlas; O77512; -.
DR Ensembl; ENSBTAT00000073288; ENSBTAP00000060343; ENSBTAG00000052095.
DR Ensembl; ENSBTAT00000082080; ENSBTAP00000058372; ENSBTAG00000052095.
DR GeneID; 280801; -.
DR KEGG; bta:280801; -.
DR CTD; 43805; -.
DR VEuPathDB; HostDB:ENSBTAG00000052095; -.
DR eggNOG; ENOG502SDQB; Eukaryota.
DR GeneTree; ENSGT00950000183133; -.
DR HOGENOM; CLU_060336_0_0_1; -.
DR InParanoid; O77512; -.
DR OMA; ALVDKFW; -.
DR OrthoDB; 1221333at2759; -.
DR TreeFam; TF353258; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000052095; Expressed in cortex of kidney and 60 other tissues.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0047961; F:glycine N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0047962; F:glycine N-benzoyltransferase activity; IBA:GO_Central.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0102080; F:phenylacetyl-coenzyme A:glycine N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006544; P:glycine metabolic process; IBA:GO_Central.
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; Direct protein sequencing; Mitochondrion;
KW Reference proteome; Transferase.
FT CHAIN 1..295
FT /note="Glycine N-phenylacetyltransferase"
FT /id="PRO_0000281873"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 48
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 48
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 182
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 182
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
SQ SEQUENCE 295 AA; 33684 MW; 4FD32FE4419AE0A2 CRC64;
MFHLQGPQLL QMLEKSLRKS LPESLKVYGT VFHMNQGNPF NLKALVDKWP DFKTVVIRPQ
EQEMADDFDH YTNTYQIYSK DLNNCQESLA TSDVINWKQH LQIQSSQSSL NEVVQNLAAT
KFVKVEHTQC ILYVMPETAR KLLPSLPETK NLPVGYGAPK AINQEMFKLS SMDPTHAALV
NKFWHFGGNE RSQRFIERCI RAFPTFCLLG PEGTPASWSL MDQTGEIRMG ATLPEYRGHG
LISHMLAVHT RALDQLGIPV YNHTDKANKI VQKVSHNLHH IAIPHGWNQW NCEPL
