ID A0A2R4T0H1_9ACTN Unreviewed; 609 AA.
AC A0A2R4T0H1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|EMBL:AVZ72609.1};
GN ORFNames=SLUN_10815 {ECO:0000313|EMBL:AVZ72609.1};
OS Streptomyces lunaelactis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1535768 {ECO:0000313|EMBL:AVZ72609.1, ECO:0000313|Proteomes:UP000244201};
RN [1] {ECO:0000313|EMBL:AVZ72609.1, ECO:0000313|Proteomes:UP000244201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM109 {ECO:0000313|EMBL:AVZ72609.1,
RC ECO:0000313|Proteomes:UP000244201};
RA Naome A., Martinet L., Maciejewska M., Anderssen S., Adam D., Tenconi E.,
RA Deflandre B., Arguelles-Arias A., Calusinska M., Copieters W., Karim L.,
RA Hanikenne M., Baurain D., van Wezel G., Smargiasso N., de Pauw E.,
RA Delfosse P., Rigali S.;
RT "Complete genome sequence of Streptomyces lunaelactis MM109T, a Ferroverdin
RT A producer isolated from cave moonmilk deposits.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR EMBL; CP026304; AVZ72609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4T0H1; -.
DR KEGG; slk:SLUN_10815; -.
DR OrthoDB; 1456at2; -.
DR Proteomes; UP000244201; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801};
KW Reference proteome {ECO:0000313|Proteomes:UP000244201};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 22..593
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 609 AA; 66690 MW; 5A566056C7E2F743 CRC64;
MKISQDVPGN ATFAQEDSLP RVPLPTLEAS CERFLAWCAP LLNPDERAAT EAEVTAFLRP
EGPGRVLHGA LEAYDAAKGV HSWLDTFWPY RYLGRRDRIA LNANFFFLFK DSGQPQVERA
AGLIAGAVNY KRQLDQGLIP PVVQRGQPQS MVQNKFLFSA TRIPGAQQDT VRSPYTEEWP
GPSEARHIVV FFRGGMFKLD VLGPDGVPHS LDDLEAGLRA VLKAGAEPTG AATSVGHLTT
MARAEWAAAR EALLACHPRN ADALDDVETA LFCVALEDFA PADTQETCDQ LLYGDRGNRW
FDKAVSFIVF ADGRAGINVE HCELDGTTIL SFTDALHSTP AEEQSQQSGA RSQGLPTLEP
IVFELDDALR AQVRSAADAF AAYGAATATS TVSFEDFGSK AAKTLRVSPD AFVQAAYQLA
HQRAKGHLGA TYESIATRQY RHGRTEAMRV VTPGIRDFVT AMEDPAADAD TRRAAFRAAA
EQHVARAKEC QLGQAPEQHL WELELIQRRR GAELGVREQP ALYRTPGWLT MRDDYLSTSS
APSANIQYFG FGSTSSRCIG VAYVLLPDRF NLYLSTPLAV ADQMRTFADR LREAVAELRE
LLGSERPGD
//
