ID I4VMC9_9GAMM Unreviewed; 574 AA.
AC I4VMC9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN ORFNames=UU9_13017 {ECO:0000313|EMBL:EIL88370.1};
OS Rhodanobacter fulvus Jip2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL88370.1, ECO:0000313|Proteomes:UP000004210};
RN [1] {ECO:0000313|EMBL:EIL88370.1, ECO:0000313|Proteomes:UP000004210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(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:EIL88370.1}.
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DR EMBL; AJXU01000054; EIL88370.1; -; Genomic_DNA.
DR RefSeq; WP_007082232.1; NZ_AJXU01000054.1.
DR AlphaFoldDB; I4VMC9; -.
DR STRING; 1163408.UU9_13017; -.
DR PATRIC; fig|1163408.3.peg.2654; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG3176; Bacteria.
DR OrthoDB; 1113830at2; -.
DR Proteomes; UP000004210; Unassembled WGS sequence.
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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Reference proteome {ECO:0000313|Proteomes:UP000004210};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 81..197
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 574 AA; 62758 MW; BE98B39DC4922CCF CRC64;
MLSIEQALVE RMPWLAQHPR IRRPMAGLFG RLADESTFNR VLDQAGAARG FDFVDRTLEL
LGTHSHVHPQ QRENIPVDGP LLVVANHPLG MQDALALLQL IGSVRRDVRV LGNDWLAVVP
QLGDLLLPVD VFGNGAASRL RGIYRALDNG EALIVFPAGE VSRVRATGVR DGRWSDGFAR
LSLRRKVPVL PIHVTARNSA AFYGLSMLAR PLSTAMLPRE AVAAGQRRIG FQIGALIDPD
ELASRSGNSP ARAAVLMRRH VYRVARGRGL IFGGQVALAH PEPVQQLVDA LAGAEKLGDL
SDGKQALLFT GSCDSAVLRE IGRLRELTFR KVGEGTGQRC DLDAYDAHYE HLLLWDPAAQ
RIVGAYRFGH GARVLSEHGM AGLYTASLFQ YSPALESRLS QGLELGRSFI APAYWRSRAL
DQLWQGIGLY LQRHREIRYL FGPVSMSVKL PREAREWIAV AHQHYFGAPG LAAARQPFVV
SPQVAERVHQ ALAGLDPQAG LGQLKHQLDA LGVSLPVLYR QYVDLMEPAG VQFLDFGEDP
DFSGCVDGLV MLDLANLKAS KRARYLGATA ASIG
//
