ID A0A2S7KRM4_9FLAO Unreviewed; 603 AA.
AC A0A2S7KRM4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=BST85_10525 {ECO:0000313|EMBL:PQB05270.1};
OS Aureitalea marina.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aureitalea.
OX NCBI_TaxID=930804 {ECO:0000313|EMBL:PQB05270.1, ECO:0000313|Proteomes:UP000239800};
RN [1] {ECO:0000313|EMBL:PQB05270.1, ECO:0000313|Proteomes:UP000239800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107741 {ECO:0000313|EMBL:PQB05270.1,
RC ECO:0000313|Proteomes:UP000239800};
RA Kumagai Y.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (NOV-2016) 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:PQB05270.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MQUB01000001; PQB05270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7KRM4; -.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000239800; 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:PQB05270.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Reference proteome {ECO:0000313|Proteomes:UP000239800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PQB05270.1}.
FT DOMAIN 81..203
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 603 AA; 69935 MW; 56E799A936011023 CRC64;
MGLVTAKEVA QAIKVDRFGF LGTAMGWTLM KILKIDTMNR IYNRNKHLED LEFMNALLDE
FEIRFEIPDE DLRRIPKNGP FITISNHPLG GIDGILLLKL LLEKRPDFKI IANFLLHRIE
PLKPYVMPVN PFENHKDVKS SMMGFKSALM HIKEGHPLGI FPAGEVSTYR DDKLLVDKPW
EVAAMKLIKK AEVPVVPIYF HAKNSKLFYR LARFNDTLRT AKLPSELLTQ KERVIKVRIG
LPIPVRDQRE HQDLDDFTDF LRKKTYVLAN PFEKKTLIES IPKTLKIPKL PKKIAGPVPV
ELMQSEIDAL KESGKRLLKS KAYEVYLAPA TEIPSILQEI GRLREITFRE VGEGTNQATD
LDDYDAYYHH MFLWDDDAKI MVGAYRMGLG SHIFSNYGID GFYLQSLFRF EPELYDMMSK
SIEMGRAFII KEYQQRPMPL FLLWKGIVHT TLRHPEHRFL IGGVSISNKF SEFSKSLMIE
FMKSNYYDPY VAQYVHPKKE YKVKLKDADK DFFFDESEAD LNKFDKLIDE VEPGSLRLPV
LIKKYIKQNA KVVAFNVDPM FNNAVDGLMY IRIADLPEST VKPVMEEFQA ELERRYNSKG
EEE
//