ID A8L3B9_FRASN Unreviewed; 632 AA.
AC A8L3B9;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|EMBL:ABW14748.1};
DE EC=2.3.1.7 {ECO:0000313|EMBL:ABW14748.1};
GN ORFNames=Franean1_5392 {ECO:0000313|EMBL:ABW14748.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW14748.1};
RN [1] {ECO:0000313|EMBL:ABW14748.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW14748.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) 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; CP000820; ABW14748.1; -; Genomic_DNA.
DR AlphaFoldDB; A8L3B9; -.
DR STRING; 298653.Franean1_5392; -.
DR KEGG; fre:Franean1_5392; -.
DR eggNOG; ENOG502Z7P4; Bacteria.
DR HOGENOM; CLU_013513_5_1_11; -.
DR GO; GO:0004092; F:carnitine O-acetyltransferase activity; IEA:UniProtKB-EC.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 49..619
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 632 AA; 68304 MW; 788B1A480A85D062 CRC64;
MTPNAPSPSS DAPEVMAAGP RQASPVASEA RSQWSTTGTF VNDDRLPRVP LPTLDDTCAR
FLQWCSPLLT PDELAATETA LAAFARPDGP GRALHAELER YDATPGVHSW LDAFWASRYL
GRRDRIALNA NFIFLFEESD AGQTARAAGL IAAALDYKLR LDAEAIEPII QRGQALSMDQ
NRFLFSTTRI PGQVQDTVRT PYSEPSPGPS TARHIVVFHR GHMFRMDVVG PEGHPHTLDD
LENGLDAILK AGAERAAPET SVGRLTTKAR AAWATSRDSL LACDPGNETA LDTVETALFC
LCLDDLTPAD AKDACDNLLH GDCGNRWFDK SVSLIVFADG SAGINIEHCG LDGTTVLSLV
DDMLGAPAAE HSARSGARSQ GVPAVRPVTF TLDDDLRADV LAAGDAFSAY AAATATATLS
FDDFGSNRAK SLRISPDAFV QLAYQLAHNR SKGLVGATYE SIATRQYRRG RTEAMRVITP
EIQAFVRVMD DPAADAATRL AALRAAADKH VTRARDCQAG RAPEQHLWEL QFIQARRGEA
LGITEHLDLF DAPGWLVTRD DYLSTSSAPS THIQYFGFGS TSNRCIGIAY VLLPDRFNVY
LSTPSVVAEQ MHSFAGHLRT ALTELQDLLE AG
//
