ID A0A0S2I3X2_9BACT Unreviewed; 597 AA.
AC A0A0S2I3X2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=L21SP5_03414 {ECO:0000313|EMBL:ALO17025.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO17025.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO17025.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO17025.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
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}.
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DR EMBL; CP013118; ALO17025.1; -; Genomic_DNA.
DR RefSeq; WP_057954359.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2I3X2; -.
DR STRING; 1307839.L21SP5_03414; -.
DR KEGG; blq:L21SP5_03414; -.
DR PATRIC; fig|1307839.3.peg.3589; -.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000064893; Chromosome.
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:ALO17025.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALO17025.1}.
FT DOMAIN 65..188
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 574..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 69213 MW; 70D1B843DB240C76 CRC64;
MSILSSSIHI TKRFLDFLLK TSGLGAEATE EKGNPEYIEK IINDIGLNIN VKDEDLDRIP
KDGPFVTISN HPFGGIDGII LLHLLLRRRP DFKILATPIL WKIYPLSEYF IRFDSSQRRS
EVKPSISGMR QVVAHIGKDK ALGFFPAGEV ASYDADTKMV ADRRWKSAYL KLLKSLEIPI
IPIYFQGKNS NLFHMVSSIH PILGSAGEFF GKKKEIRVRI GSPINASETA GIDDLDKYGR
YLRAKTYALE SEIEVKKFFK TALKREKEPA KIIDAVPTET IKAELNRIKE YELFTSEKYT
VYCAPTLLIP YIHREIGRVR EITFRAVGEG TNRSIDIDEF DLYYNQLFIW DNEEEQLIGA
YRVGKGKEII AQFGVKGFYT RSLFKIHKDF TPILKESIEL GRSFITEPYQ RKPMSLFLLW
KGILYFLLKH PEYRYLIGPV SISNQFSKFS KDLIIKFLKQ NHFNHELGRL ITPRKKFKVQ
SRYDTDIVLE NTRNDINKVD RFISDIEPTN YRMPVLLKKY LKQNAKIIGF NIDPKFNNAL
DGLVILDLYE VPFNMIESLS KEVNDDSILD RFKMTEDEKR EEEEVKNTNK AEHQKQK
//
