ID A0A0F5ZUP6_9GAMM Unreviewed; 578 AA.
AC A0A0F5ZUP6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=RN22_16585 {ECO:0000313|EMBL:KKD59354.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD59354.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD59354.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD59354.1,
RC ECO:0000313|Proteomes:UP000033732};
RA Adrian T.-G.-S., Chan K.-G.;
RT "Genome sequencing of Grimontia sp. AD028.";
RL Submitted (APR-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:KKD59354.1}.
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DR EMBL; LASY01000074; KKD59354.1; -; Genomic_DNA.
DR RefSeq; WP_046305906.1; NZ_LASY01000074.1.
DR AlphaFoldDB; A0A0F5ZUP6; -.
DR PATRIC; fig|1581149.3.peg.4234; -.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000033732; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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 ECO:0000313|EMBL:KKD59354.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKD59354.1}.
FT DOMAIN 81..198
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 578 AA; 65952 MW; 6C10106662D624B7 CRC64;
MFSIDDVITK NYPKIADKRW ISRPVSSTLR RLLHEEAFQS FAEKYPYLRG FEFVEQVLDY
FHFSHATSDR ERERIPSTGR VVIIANHPIG SLDGLALLKL VREIRPDVKA VANNLLMQIE
PMHNCLLPVN NMSGKTPKEN LRKIDEWLQN DGALIIFPAG EVSRFSPTGV KDKAWHHGFL
KMATKAKAPI LPIHVDGRNS AVFYGASMVY KPLSTLLLVN EMFGQENNTI NLTIGEAIPF
ASYHASANLP PKTRVKLFRK HLYSIAKGKP GEFPTESAIA SPEPRLKLAK ELEQSERLGE
TPDGKSIYLY RYKDESHVMR EIGRLREVAF RAVGEGTGQR RDIDKYDQHY FHLVLWDPKA
MDIVGAYRFC DTQAVIAQHG LKAVYTHTLF DYGDGMSDVL NKGLELGRSF VQPKYWGKRS
LDYLWLGIGA FLAKHPHYRY LFGPVTISNA MPQAAKELLI FFYSTYFGAH ATIARSKRPF
NIDSQKEHEL LVHFCGDDYQ KDLKTLKMLL DNLGTGIPTL YKQYSELCEP GGVQFLDFSI
DPDFADCIDG LVMVDMTKLK EKKRQRYISP HLREIELV
//
