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Database: UniProt
Entry: D4E648_SEROD
LinkDB: D4E648_SEROD
Original site: D4E648_SEROD 
ID   D4E648_SEROD            Unreviewed;       573 AA.
AC   D4E648;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000256|ARBA:ARBA00039866};
DE            EC=2.3.2.30 {ECO:0000256|ARBA:ARBA00039058};
GN   ORFNames=HMPREF0758_3648 {ECO:0000313|EMBL:EFE94777.1};
OS   Serratia odorifera DSM 4582.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE94777.1, ECO:0000313|Proteomes:UP000005723};
RN   [1] {ECO:0000313|EMBL:EFE94777.1, ECO:0000313|Proteomes:UP000005723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE94777.1,
RC   ECO:0000313|Proteomes:UP000005723};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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:EFE94777.1}.
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DR   EMBL; ADBY01000051; EFE94777.1; -; Genomic_DNA.
DR   RefSeq; WP_004962730.1; NZ_GG753567.1.
DR   AlphaFoldDB; D4E648; -.
DR   STRING; 667129.HMPREF0758_3648; -.
DR   HOGENOM; CLU_033329_1_0_6; -.
DR   OrthoDB; 1113830at2; -.
DR   Proteomes; UP000005723; 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:EFE94777.1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFE94777.1}.
FT   DOMAIN          77..194
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   573 AA;  64947 MW;  6FA694741C77047B CRC64;
     MFSLDTLLQD AFPHRNPPAW QRSLLRNLLF EKEFKQFAAE YPHLKGFDLI EQVVDYFKLS
     CELVDGDLEN IPSQGPVVLV ANHPIGSLDG LVLLRAVAAV RRDVKVVASQ ILSYIEPLRS
     LFVPVDNVEY KTNRRQIEAM QAQLDNQGVL IVFPAGEVSR ISPQGIRDGH WHTGFVRLAA
     KARAPIVPIH ISARNSNLFY FASLVYRPLS TLLLVREMFQ QQGGRIKLRI GGRIPFASWH
     DGHTSAHELA ERFRRHVYRL GQGKPGLFAS ESPIALPENR LELRKALSAC ERLGKTPDGK
     IIFLYRRHDE TRSPILRELG RLREIAFRAV GEGSGRRRDL DSYDDDYYHL VLWDEDELDI
     VGAYRFIPTA EQLANKGLEG IYSNSLFHYD RDMAPILEQG IELGRSFIQP AYWGKRGLDY
     LWLGIGAYLA TYPQYRYLFG PVSISGGMPV AARDLLIAFY RLYFSSDSTL AQSRQPYPAS
     LPQVLAQFSG DNYQADLVRL KSLLSNIGCS IPTLYKQYSE LCEPGGVQFI DFGTDPAFNN
     CIDGLVLVDL LRLKPARYQR YIAVHQPDES TRA
//
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