ID A1S492_SHEAM Unreviewed; 586 AA.
AC A1S492;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN OrderedLocusNames=Sama_0991 {ECO:0000313|EMBL:ABL99198.1};
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABL99198.1, ECO:0000313|Proteomes:UP000009175};
RN [1] {ECO:0000313|EMBL:ABL99198.1, ECO:0000313|Proteomes:UP000009175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-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; CP000507; ABL99198.1; -; Genomic_DNA.
DR RefSeq; WP_011759107.1; NC_008700.1.
DR AlphaFoldDB; A1S492; -.
DR STRING; 326297.Sama_0991; -.
DR KEGG; saz:Sama_0991; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG3176; Bacteria.
DR HOGENOM; CLU_033329_1_0_6; -.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000009175; 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:ABL99198.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Reference proteome {ECO:0000313|Proteomes:UP000009175};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABL99198.1}.
FT DOMAIN 82..199
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 586 AA; 65715 MW; 6922FBCFAD695E3E CRC64;
MIFTVDNLID TRLPAISASP WLKRPVSAAL RFLLHEEECN RIAAEFAFMQ GVDFAGAVLE
TLNFSFTVPD SDLDNIPAKG RVVIFANHPI GSLDALAMIK LIGEIRPDIK VVANEILMAI
EPLHPILLPV RNMGGGTPKH HLEAIHRHLQ NDGALLIFPA GEVSRLRPNG VRDTLWQSGF
LKIALACDAP LLPLFADARN SATFYGTSMI YKPLSTLLLV KEMFRQKQRT MPIRIGELIA
LDALKAKDFD LKTKVTLLKN HLYRIGKNRP PLFKTQSPIA RPECRAELKA ALGACEHLGN
TQDGKTIYLY QHQGSNPIMR EIGRLREQAF RAVGEGTGKR RDIDAFDSHY LHLVLWDKEA
LEVVGAYRFA SASKLHQELG ANSLYSQSLF DFTDAFAPCF AEGLELGRSF VQPRYWGKRS
LDYLWFGIGA FLARNPQYRY LFGPVSISGQ LPLAAREMLV DFYGRFYGAN TQLASPKQAF
RLSDERRREL DKLYEGLPME DAFKRLKHTL SGMGVAVPTL YKQYTELCHE DGVSFAAFSV
DPDFGHCVDG LVTVDLTRLK DKKRERYLGV HRQDNAQLVL ADGEGV
//
