GLYAT_PONAB
ID GLYAT_PONAB Reviewed; 296 AA.
AC Q5RFP0; Q5R5B4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Glycine N-acyltransferase;
DE EC=2.3.1.13 {ECO:0000250|UniProtKB:Q6IB77};
DE AltName: Full=Acyl-CoA:glycine N-acyltransferase;
DE Short=AAc;
DE AltName: Full=Aralkyl acyl-CoA N-acyltransferase;
DE AltName: Full=Aralkyl acyl-CoA:amino acid N-acyltransferase;
DE AltName: Full=Benzoyl-coenzyme A:glycine N-acyltransferase;
DE AltName: Full=Glycine N-benzoyltransferase;
DE EC=2.3.1.71 {ECO:0000250|UniProtKB:Q6IB77};
GN Name=GLYAT;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q6IB77}.
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:0000250|UniProtKB:Q6IB77};
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:0000250|UniProtKB:Q6IB77};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6IB77}.
CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CR857113; CAH89417.1; -; mRNA.
DR EMBL; CR860949; CAH93052.1; -; mRNA.
DR RefSeq; NP_001126806.1; NM_001133334.1.
DR AlphaFoldDB; Q5RFP0; -.
DR SMR; Q5RFP0; -.
DR STRING; 9601.ENSPPYP00000003731; -.
DR GeneID; 100173810; -.
DR KEGG; pon:100173810; -.
DR CTD; 10249; -.
DR eggNOG; ENOG502SDQB; Eukaryota.
DR InParanoid; Q5RFP0; -.
DR OrthoDB; 1221333at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0047961; F:glycine N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047962; F:glycine N-benzoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006544; P:glycine metabolic process; ISS:UniProtKB.
DR GO; GO:0032787; P:monocarboxylic acid metabolic process; ISS: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 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Detoxification; Mitochondrion;
KW Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Glycine N-acyltransferase"
FT /id="PRO_0000281871"
FT MOD_RES 16
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 16
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 127
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 127
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 141
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 141
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 159
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 169
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 256
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT MOD_RES 256
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91XE0"
FT CONFLICT 44
FT /note="K -> T (in Ref. 1; CAH93052)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="Q -> L (in Ref. 1; CAH93052)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> N (in Ref. 1; CAH93052)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="F -> L (in Ref. 1; CAH93052)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 33855 MW; 0D03375446A74EDF CRC64;
MMLPLQGAQM LQVLEKSLRR SLPASLKVYG TVFHINHGNP FNLKAVVDKW PDFNTVVVCP
QEQDMTDDLD HYTNTYQIYS KDPQNCQEFL GSPELINWKQ HLQIQSSQPS LNEAIQNLAV
IKSFKVKQTQ RILYMAAETA KELAPFLLKS KILSPSGGKP KAINQEMFKL SSMDVTHAQL
VSKFWHFGGN ERSQRFIERC IQTFPTCCLL GPEGTPVCWD LMDQTGEMRM AGTLPEYRLH
GLVTYVIYSH AQKLGKLGFP VYSHVDYSNE AMQKMSYTLQ HVPIPRSWNQ WNCVPL
