ID A0A023BPU8_9FLAO Unreviewed; 602 AA.
AC A0A023BPU8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=ATO12_05160 {ECO:0000313|EMBL:EZH72006.1};
OS Aquimarina atlantica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH72006.1, ECO:0000313|Proteomes:UP000023541};
RN [1] {ECO:0000313|EMBL:EZH72006.1, ECO:0000313|Proteomes:UP000023541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH72006.1,
RC ECO:0000313|Proteomes:UP000023541};
RA Lai Q.;
RT "Aquimarina sp. 22II-S11-z7 Genome Sequencing.";
RL Submitted (APR-2014) 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:EZH72006.1}.
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DR EMBL; AQRA01000010; EZH72006.1; -; Genomic_DNA.
DR RefSeq; WP_034246322.1; NZ_AQRA01000010.1.
DR AlphaFoldDB; A0A023BPU8; -.
DR STRING; 1317122.ATO12_05160; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG3176; Bacteria.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000023541; 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:EZH72006.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Reference proteome {ECO:0000313|Proteomes:UP000023541};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EZH72006.1}.
FT DOMAIN 81..203
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 602 AA; 69903 MW; 9834A655893053CE CRC64;
MPIVTAREVA AGLKMDKFGF IGTFIGWVIL KVTRLSKVNR QYDKISHLKD LDFLTKTLEI
HNVNYEIPEE DLKRLPKNGA FITLSNHPLG GLDGVLLLKL MLEHRSDYKI IANFLLHSFS
PLKPYIMPVN PFEDRKEAKS SLKGIKEAIL HLREGKPLGI FPAGEVSTFK EGKNYVDKPW
EPSAMRLVQK AKVPVIPIYF HARNSRLFYR LASISDILRT AKLPSELFSQ ENKVIKVRIG
NPVSVKDQEE HTNLEDFTNF LRKKTYMLAN PFEKKTLRES IPQNLKLPKS PKEIAVEGNI
NAIESELQYC REHDKRLLIS KNYEVFLAKK QHIPNVVREI GRLREITFRA IGEGTNNSLD
LDPFDEYYHH MFLWDNEAKR MVGAYRMGMG SQIYANRGID GFYLQDLFRF EPELHKMMNE
SIEMGRAFII KEYQQRPMPL FLLWKGIVHC TLRFPEHKYL IGGVSISNKF SNFSKSLMIE
FMKSHYYDPY VAQYVRPKKE FKVKLKDADK DFVFDESKSD LNKFDKIIDE VEPGSLRIPV
LIKKYIKQNA KVVAFNVDPL FNNAVDGLMY IRIADLPDST VKPVMEEFQA ELEQKYFKNG
DK
//