ID   Q081F2_SHEFN            Unreviewed;       579 AA.
AC   Q081F2;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE            EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN   OrderedLocusNames=Sfri_2267 {ECO:0000313|EMBL:ABI72113.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI72113.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI72113.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI72113.1,
RC   ECO:0000313|Proteomes:UP000000684};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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; CP000447; ABI72113.1; -; Genomic_DNA.
DR   RefSeq; WP_011637722.1; NC_008345.1.
DR   AlphaFoldDB; Q081F2; -.
DR   STRING; 318167.Sfri_2267; -.
DR   KEGG; sfr:Sfri_2267; -.
DR   eggNOG; COG0204; Bacteria.
DR   eggNOG; COG3176; Bacteria.
DR   HOGENOM; CLU_033329_1_0_6; -.
DR   OrthoDB; 1113830at2; -.
DR   Proteomes; UP000000684; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.30; -; 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:ABI72113.1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000684};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABI72113.1}.
FT   DOMAIN          82..199
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   579 AA;  66161 MW;  97CAB9452E53A4C3 CRC64;
     MIFTVDNVVE KNLPNVHNKP WLAVPTKAML RYLLHEKQCN DIANEHAHLS GVDFVEQILA
     CLNFSYSVPN NEIENIPIEG RVVIYANHPI GSLDALALIK LISQVRPDIK VVANELLMAI
     KPLHSILLPV RNMTGGTPKQ HLNEIHHHLK REGAVLIFPS GEVSRLRPTG VTDLHWHSGF
     LKMARACNAP LLPMYVDAKN SATFYGASMI YKPLATLLLV KEMFKQMDHV MPVRIGQLIA
     KEVVSTQDFP LKTKVNLLKN HLYRIGKNRS PLFITQNAIA HPEKRSELQQ ALQQCELLGK
     TQDNKQIYLY KHTHSSAIMR EIGRLREIAF RAVGEGTGKR RDTDKYDNHY FHLVLWDKDE
     LEIVGAYRFA SAKMLHESIG ENALYSQSLF EYHDAFAPYF DQGLELGRSF VQPKYWGRRS
     LEYLWQGIGA FLIKNPQYRY LFGPVSLSDS LPVPAKEMLV FFYQHHFATK HVLATSFNSY
     QFTDERQHQL HQLFNGNDYA DNFKILKRTL SNMGVSVPTL FKQYGELCDN NGVQFLDFGI
     DAEFGDCIDG LVLVDIHQLK PIKYQKYLAG HLPENKIAS
//