ID A0A0Q4FV88_9SPHI Unreviewed; 583 AA.
AC A0A0Q4FV88;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=ASE74_11590 {ECO:0000313|EMBL:KQM64650.1};
OS Pedobacter sp. Leaf216.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1735684 {ECO:0000313|EMBL:KQM64650.1, ECO:0000313|Proteomes:UP000051744};
RN [1] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Garrido-Oter R., Mueller D.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + L-ornithine = a lyso-ornithine
CC lipid + H(+) + holo-[ACP]; Xref=Rhea:RHEA:20633, Rhea:RHEA-COMP:9685,
CC Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:46911,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78827, ChEBI:CHEBI:138482;
CC EC=2.3.2.30; Evidence={ECO:0000256|ARBA:ARBA00036203};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20634;
CC Evidence={ECO:0000256|ARBA:ARBA00036203};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. OlsB subfamily.
CC {ECO:0000256|ARBA:ARBA00038095}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQM64650.1}.
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DR EMBL; LMKM01000037; KQM64650.1; -; Genomic_DNA.
DR RefSeq; WP_055914902.1; NZ_LMKM01000037.1.
DR AlphaFoldDB; A0A0Q4FV88; -.
DR STRING; 1735684.ASE74_11590; -.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000051744; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd07986; LPLAT_ACT14924-like; 1.
DR InterPro; IPR045746; ACT14924-like_Acyltransf_dom.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR37323; GCN5-RELATED N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR37323:SF1; L-ORNITHINE N(ALPHA)-ACYLTRANSFERASE; 1.
DR Pfam; PF13444; Acetyltransf_5; 1.
DR Pfam; PF19576; Acyltransf_2; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 79..201
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 583 AA; 66671 MW; BFB6F700A8D0AFBE CRC64;
MKIITTSEFA KATKIDKLGV PGLAGLMMEI MKLNDINDVF AQNQHFKGLE FVDKILETIG
VSIEFDDDDL NSIPKTGPFI AIANHPYGGV EGLALVKLLC TVRPDAKVMV NFILKKIPNL
DEFFVAVNPF ENVQHSSSIS GLKTTFDLLR NGIPIGIFPA GEVSTFKLDA QQVTDRMWHP
VVGKLIAKAK VPVVPIYFHG NNGVFFNILS FIHPTLRTAK LPSEFLNKHG RTIKVRIGKP
IAISEISHMN SSNKLMDFLR ARTYALGIGL DTEKKLFNPL NLFKIKKKPA EVIEETSRLL
IKSEVEKLED FKVWTEKNYE VYIVPTLKIP NILREIGRLR EITFREVGEG TNKKIDLDNY
DIYYNHLFIW DRDLENIVGA YRIGKGDEIL ESMGRRGFYL SELFKMKDQF YPMLRQGIEL
GRSWIRKEYQ GKPLPLFLLW KGILKYLIDN PQYRYMFGPV SISNNFSKFS KALIVDYITK
NHFDYEMAKY VKPRNKFKAD LLPISTDTLV DSSESFKDLD SIIGDIENSH IKIPVLLRQY
MNLNAKIISF NIDPKFSDCL DGFLVVDTHN IPPEMLEKLG KNL
//