ID A0A1V3PVL5_9GAMM Unreviewed; 570 AA.
AC A0A1V3PVL5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=B0E48_14205 {ECO:0000313|EMBL:OOG54449.1};
OS Rhodanobacter sp. C03.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1945858 {ECO:0000313|EMBL:OOG54449.1, ECO:0000313|Proteomes:UP000189128};
RN [1] {ECO:0000313|EMBL:OOG54449.1, ECO:0000313|Proteomes:UP000189128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C03 {ECO:0000313|EMBL:OOG54449.1,
RC ECO:0000313|Proteomes:UP000189128};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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:OOG54449.1}.
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DR EMBL; MUNT01000010; OOG54449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3PVL5; -.
DR STRING; 1945858.B0E48_14205; -.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000189128; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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:OOG54449.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OOG54449.1}.
FT DOMAIN 81..197
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 570 AA; 62443 MW; DF8C039B2B76511B CRC64;
MLSIEQSLVE RLPWLAQYPA IRRPVAGMLG RLADEDGFNR VLDRVGTATG FDFVERVLDV
LGTSYHVNSR EREHIPIDGP LLVVANHPLG MQDALALLQL IGSVRSDVRM LGNDWLATVP
QLGRLLLPVD VFGKGAASRL RGIYRALDNG EALIVFPAGE VSRMRADGVR DGRWSDGFAR
LSLRRKVPVL PVHVAARNST MFYGMSMLAR PLSTAMLPRE AVASGSRRIG FSIGALVTPA
ELEQRSAGSS TQAARLMRRH VYRVGRHRGL IFGGQAPLAH PEPAAQVAAE LARAEKLADL
GDGKQALLFK GVADSTVLRE IGRLRELTFR KVGEGTGERR DLDAWDPHYE HLVLWDPQAL
RIVGAYRLGH GGRLICERGM AGLYTSSLFH YSPALESRLA QGLELGRSFI APAYWRSRAL
DQLWQGIGLY LQRHPELRYL FGPVSMSVSL PREAREWIAA AHQHYFGAPG LAAARQPFVI
SAEVIRGVQL ALAGLDASAG LGKLKHHLDA LGVSLPVLYR QYVDLVEPDG VQFLDFGEDP
GFSGCVDGLV MLDLAALKPL KRARYLGKSA
//