ID W7QU67_9ALTE Unreviewed; 569 AA.
AC W7QU67;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, 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=DS2_14514 {ECO:0000313|EMBL:EWH08995.1};
OS Catenovulum agarivorans DS-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH08995.1, ECO:0000313|Proteomes:UP000019276};
RN [1] {ECO:0000313|EMBL:EWH08995.1, ECO:0000313|Proteomes:UP000019276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH08995.1,
RC ECO:0000313|Proteomes:UP000019276};
RX PubMed=24604650;
RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL Genome Announc. 2:e00144-14(2014).
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:EWH08995.1}.
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DR EMBL; ARZY01000031; EWH08995.1; -; Genomic_DNA.
DR RefSeq; WP_035015556.1; NZ_ARZY01000031.1.
DR AlphaFoldDB; W7QU67; -.
DR STRING; 1328313.DS2_14514; -.
DR PATRIC; fig|1328313.3.peg.2959; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG3176; Bacteria.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000019276; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07986; LPLAT_ACT14924-like; 1.
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:EWH08995.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Reference proteome {ECO:0000313|Proteomes:UP000019276};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EWH08995.1}.
FT DOMAIN 81..198
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 569 AA; 65573 MW; 62DA50D5AD78F963 CRC64;
MFTVEEVIEK NLPQLQKHPI LSTLTRKVLK RLLHEQEFIE FADHYPHLRG LDFVEQSLEY
FDFSYTISAR DLERIPSQGR CVIIANHPIG SLDGLALIKL VSEVRKDFKV VANELLMAIE
PLRPMLLPVN NMAGRTAREN IRGIQDYLNN NGAVIIFPAG EVSRLKPAGI RDSRWNGGFL
KLAQATQSPI LPIHVQGKNS NSFYLLSMLY KPLSTLFLVN EMFKQQDKNM PVRVGELIPY
DSFKGSQLTN KEKIRLFQRH LYRIGKQKKG CFVTESAIAR PEHRQELAKA IYNCELLGQT
ADNKDIYLYK FEDSSPIMRE IGRLRELSFR AVGEGSGKKR DIDKYDAYYE HLILWDKQEQ
EIVGAYRLGQ TLEIIQAHGQ HGLYTDSLFI YDQQMQKYFE HGLELGRSFV QPKYWGMRSL
DYLWYGIGAF LKKHPNIRYL FGPVSMSNSM PKPAKDLMVY FYKLYFQHQE VIASSKQPYK
IPNDVISVLK TEFTGDNYKT DFAKLKSMLA NMGTSVPTLY KQYSELCEED GVKFLDFGVD
PDFADCIDGL VLVDITKLKA NKKARYLAK
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