ID K2QK65_9FLAO Unreviewed; 607 AA.
AC K2QK65;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=I215_08732 {ECO:0000313|EMBL:EKF55102.1};
OS Galbibacter marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF55102.1, ECO:0000313|Proteomes:UP000007364};
RN [1] {ECO:0000313|EMBL:EKF55102.1, ECO:0000313|Proteomes:UP000007364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX PubMed=23209227; DOI=10.1128/JB.01852-12;
RA Lai Q., Li C., Shao Z.;
RT "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL J. Bacteriol. 194:6973-6973(2012).
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:EKF55102.1}.
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DR EMBL; AMSG01000010; EKF55102.1; -; Genomic_DNA.
DR RefSeq; WP_008991595.1; NZ_AMSG01000010.1.
DR AlphaFoldDB; K2QK65; -.
DR STRING; 555500.I215_08732; -.
DR PATRIC; fig|555500.3.peg.1804; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG3176; Bacteria.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000007364; 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:UP000007364};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 81..203
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 607 AA; 70320 MW; 54E81F8939419AC5 CRC64;
MGLVSAKEVA KVIKADKLGV LGTFSGWFLM KVLNLSTLNA VYDKHKDKQD LHFLNSILEE
FEINFEIPEE DFKRIPKDGA YITVSNHPLG GIDGILLLKL LLEHRSDYKI IANFLLHRIV
PLKPYIMPVN PFETHKDAKS SISGFKQALS HLKQGHPLGI FPAGEVSTNK DGNLVVDKPW
EPAAMKLIKK AEVPVVPIYF HAKNSNLFYR LSNFSDTLRT AKLPSELLNQ RNRVIRVRIG
RPISVEAQQE FDNLPEFTDF LRRKTYMLSN SYDQDRLLDK VTTSLKFPRS PKEIITPVDK
TLMEQDVDKL REEDLRLFQS KNYEVFLSTA QKMPNIIREI GRLREITFRA VGEGTNRAID
LDEFDLYYHH LFLWDNKEKA IVGAYRMGLG SEIFKSRGID GFYLQDLFKF EPELYRMMSE
SIEMGRAFIV SDYQQKPMPL FLLWKGIVHT TLRHPEHKYL IGGVSISNQF TNFSKSLMIE
FMKSHYWDPY VAQYVRPKKE FKVKLKDADK EFVFDETASD LNKFDRLIDE VEPGSLRLPV
LIKKYIKQNA KVVAFNVDPL FNNSVDGLMY IKIADLPEST VKPVMEEFQA ELERKHIEEL
KNNHNES
//