ID A0A0N9N086_9ACTN Unreviewed; 422 AA.
AC A0A0N9N086;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ALG83468.1};
GN ORFNames=ACH46_01770 {ECO:0000313|EMBL:ALG83468.1};
OS Gordonia phthalatica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG83468.1, ECO:0000313|Proteomes:UP000063789};
RN [1] {ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA Jin D., Kong X., Bai Z.;
RT "Complete genome sequence and metabolic analysis of phthalate degradation
RT pathway in Gordonia sp. QH-11.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALG83468.1, ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG83468.1,
RC ECO:0000313|Proteomes:UP000063789};
RX PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CP011853; ALG83468.1; -; Genomic_DNA.
DR RefSeq; WP_062391419.1; NZ_CP011853.1.
DR AlphaFoldDB; A0A0N9N086; -.
DR STRING; 1136941.ACH46_01770; -.
DR KEGG; goq:ACH46_01770; -.
DR PATRIC; fig|1136941.3.peg.354; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000063789; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003333; CMAS.
DR InterPro; IPR020803; PKS_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43667; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR PANTHER; PTHR43667:SF1; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR Pfam; PF02353; CMAS; 1.
DR PIRSF; PIRSF003085; CMAS; 1.
DR SMART; SM00828; PKS_MT; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 150..411
FT /note="Polyketide synthase methyltransferase"
FT /evidence="ECO:0000259|SMART:SM00828"
FT ACT_SITE 387
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 422 AA; 47606 MW; E8FB531CFEEC6984 CRC64;
MKLAQIIETL VGRDLAVRIT AYDGSSAGPE NAEFGLDLKT PRGTTYLVTA PGDLGLARAY
VSGDLELIGA HPGDPYGALQ ALAGDLKFRK PNPVELAQIA RSIGREHFKL IPPPPQESLP
RWRRFAEGLR HSRERDAEVI HYHYDVSNRF YELVLGESMT YTCAVYPTPD ATLEEAQENK
YRLVFDKLNL QPGDRLLDMG CGWGGMVRYA ARRGVHALGV TLSSEQAQWA QEAIEREGLS
EFAEVRYSDY RDVPESDFDA ISSIGLTEHI GVANYPKYFS FMRDKVRSGG LILNHCITRP
DNRTRSKAGP FIDRYVFPDG ELTGSGTIIS RMQDVSRLEV LHEENFRHHY ALTLRDWNKN
LVKNWDEAVA EVGEGTARLW GLYMAGCRIG FERDIVQLHH VLATKLQLDS TTNLPMRPWW
EP
//
