ID   C1DVW1_SULAA            Unreviewed;       531 AA.
AC   C1DVW1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE            EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN   OrderedLocusNames=SULAZ_1279 {ECO:0000313|EMBL:ACN98821.1};
OS   Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium.
OX   NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN98821.1, ECO:0000313|Proteomes:UP000001369};
RN   [1] {ECO:0000313|EMBL:ACN98821.1, ECO:0000313|Proteomes:UP000001369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Az-Fu1 / DSM 15241 / OCM 825
RC   {ECO:0000313|Proteomes:UP000001369};
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001229; ACN98821.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1DVW1; -.
DR   STRING; 204536.SULAZ_1279; -.
DR   KEGG; saf:SULAZ_1279; -.
DR   eggNOG; COG0204; Bacteria.
DR   eggNOG; COG3176; Bacteria.
DR   HOGENOM; CLU_512778_0_0_0; -.
DR   Proteomes; UP000001369; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   Gene3D; 3.40.630.30; -; 1.
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; PF01553; Acyltransferase; 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:ACN98821.1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001369};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACN98821.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        280..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          347..459
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   531 AA;  61893 MW;  1E0C51927AC8E8B0 CRC64;
     MIAINKIKNV KNIPVSFYKY KIKNFKSKVN IHIETNSYVV KTAKTMNELL DLLKLRFEVF
     LEGKRKMIPL DFDEYDLVAD HIMILDKKSG KPVGTYRLIS SIFSNKFYSE TEFYIDKIKK
     LNGNILEMGR AAIKKDYRNG ITIALLWKGI AQYVKQTNSK FLFGCSSVYT TDPVEAAYLY
     LYLKKNYFKE SLLCEVKPNY VMPNFQKYLN LLENLNPDFK KAEEFIPPLL KAYLNAGAFV
     CSYPALDREF NCIDFITVLN TDNLAKTFER KYKKVKYIKF LHKLGVFLVL TLLFITSSTF
     IYFFTVDKKK RLKKLVKNSN FYRDLALKLF NVKVYINNFN LNTEENYIIT PNHLSYLDII
     VLKNNDKNLF VSTHEVKETF LFGKVAEFGG SVFINRQSKN GIKQEIETLK EVLKEGFSIV
     IFLEGTTSNG ETVLPFKSSF VEIAFELGVK IVPTCIRYRT VNGEEINEKN RDLIFYYGDM
     NLFKHVFNFL LNVNSVEVEV IFLNPINPSD FKDRKELSKY LHSEILKCYT G
//