ID A0A285X2S2_9FLAO Unreviewed; 612 AA.
AC A0A285X2S2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=SAMN06296241_1168 {ECO:0000313|EMBL:SOC79637.1};
OS Salinimicrobium sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salinimicrobium.
OX NCBI_TaxID=1343891 {ECO:0000313|EMBL:SOC79637.1, ECO:0000313|Proteomes:UP000219193};
RN [1] {ECO:0000313|Proteomes:UP000219193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12641 {ECO:0000313|Proteomes:UP000219193};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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}.
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DR EMBL; OCMF01000001; SOC79637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285X2S2; -.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000219193; 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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Reference proteome {ECO:0000313|Proteomes:UP000219193};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 81..203
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 612 AA; 70962 MW; E18AEED87EF9591C CRC64;
MGIVSAKEVA KVMNLDKLGF LGTSMGWVLL KTTKLSVINK EYEKRKNLPA PQFIDSLLKA
FEIDFEIPQE DLKRIPKSGP FITISNHPLG GIDGMILLKL LLSQREDFKV IANFLLQRIE
PLQPYIMPVN PFEEHKEVQS STKGIKEAIM HLREGKPLGI FPAGEVSTYR EERRIVDRPW
DPAAMKLILK AKVPVIPIYF HAKNSTFFYR LASVSDILRT AKLPSEMLSQ KKRKIKVRIG
NAINPQDIQE ITTVESLTAF LRRKTYMLAN AFEKKPFLKS IPKNFKIPKQ PKKIVEETQC
DLMLEEVETC RKLDKRLLES KNYEVFLAKK EIIPNILKEI GRLREITFRA IGEGTNNPVD
LDKFDDYYYH MFLWDNEARK IAGAYRMGMG AEIFAEHGIQ GFYLQDLFRF EPELYKMMSE
SIEMGRAFIT KEYQQRPMPL FLLWKGIVHC TLRFPKHKYL IGGVSISNKF SNFSKSLMIE
FMRSHYYDPY VAQYVRPKKE FKVKLKDGDK DFIFDETQAD LNKFDKIIDE VEPGSMRLPV
LIKKYIKQNA KVVAFNVDPL FNDAIDGLMY IKIADLPEST VRPVMEEFQQ ELERKVTEMR
KNEAAAKESG ES
//