ID F3Z1F7_DESAF Unreviewed; 603 AA.
AC F3Z1F7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=Desaf_1652 {ECO:0000313|EMBL:EGJ49988.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49988.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ49988.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49988.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
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; CP003221; EGJ49988.1; -; Genomic_DNA.
DR RefSeq; WP_014259754.1; NC_016629.1.
DR AlphaFoldDB; F3Z1F7; -.
DR STRING; 690850.Desaf_1652; -.
DR KEGG; daf:Desaf_1652; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG3176; Bacteria.
DR HOGENOM; CLU_033329_1_0_7; -.
DR Proteomes; UP000007844; Chromosome.
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:EGJ49988.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGJ49988.1}.
FT DOMAIN 84..207
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 603 AA; 68134 MW; BCB275063C456E65 CRC64;
MPQAHQEKLL RLDVPIRGSI KKRLFHLVRP PLSRLLCLSK LNDIYSAVDK RDLPTFMTDS
LRHMGVRINL SFEDATRIPT QGPVLVVANH PFGAIEGVVL GSVLRSARPD VKLMANYMLS
VIPEMRELLI QVDPFGAGGS HKRNIGPLKE SLRWLKSGGM LGVFPAGEVS SLNVRKRSVE
DPQWSTTIAR MARKAGVPVL PVYFDGCNSS LFQMLGLIHP RLRTAMLPRE LLNRREGVID
VRIGSLIQPS KFESFETDEQ LVDFLRQRTY ILKHRKPEVA PAARIARKAV VGEPIAPPVA
PALIEAEIAS LPKKSILWEN NEYTLFLGRR SELPNTVIEL GRLREETFRE VGEGTGKASD
LDQYDDYYWH LCLWHRQDRE IVGSYRLGPT DDILARVGPS GLYTNTLFRY RREFLEQISP
ALELGRSFVR KKYQKSYLPL LTLWKGIGIF LGRNMQYRYL FGPVSISNSY APFSKALMVK
FLNTHARERV GGMVKAKLPP RLDAGPNWRE LCRLCCNIED LGDFISEIEK DRKGVPVLLR
QYLKLGGKIL AFNVDPEFAG ALDGLILVDL LQTDPKTLAK HMGVEAARQF LTLHKGERTD
KAS
//
