ID X5DIL4_9CORY Unreviewed; 455 AA.
AC X5DIL4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:AHW62893.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:AHW62893.1};
GN Name=cma {ECO:0000313|EMBL:AHW62893.1};
GN ORFNames=CGLY_02225 {ECO:0000313|EMBL:AHW62893.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW62893.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW62893.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW62893.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CP006842; AHW62893.1; -; Genomic_DNA.
DR RefSeq; WP_038545782.1; NZ_CP006842.1.
DR AlphaFoldDB; X5DIL4; -.
DR STRING; 1404245.CGLY_02225; -.
DR KEGG; cgy:CGLY_02225; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_6_2_11; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000023703; Chromosome.
DR GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IEA:UniProtKB-EC.
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 Methyltransferase {ECO:0000313|EMBL:AHW62893.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023703};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHW62893.1}.
FT DOMAIN 161..414
FT /note="Polyketide synthase methyltransferase"
FT /evidence="ECO:0000259|SMART:SM00828"
SQ SEQUENCE 455 AA; 50934 MW; 49CD00DE6FCE45CB CRC64;
MSRGFTPLTV GQIVDKVITP PAPFRVTAFD GSTAGPADAE LALEITSPDA LAYIVTAPGD
LGLARAYITG SLRVTGDEPG HPYLVFDHLQ HLYDQIRRPS AKDLLDIARS LKAMGAIKVQ
PAPEQETLPG WKRAILEGLS RHSPERDKEV VSRHYDVGND FYELFLGDSM AYTCAYYPEF
DGENQVTGPT GGWRYDDWEK GPTANGPLTQ AQDNKHRLVF DKLRLNPGDR LLDVGCGWGG
MVRYAARHGV KAIGVTLSRE QYEWGKAKIE EEGLQDLAEV RCMDYRDVPE SDFDAVSAIG
ILEHIGVPNY EDYFTRLFAK LRPGGRMLNH CITRPHNRKT KTGQFIDRYI FPDGELTGSG
RIITIMQDTG FDVVHEENLR PHYQRTLHDW CELLATNWDQ AVHLVGEETA RLFGLYMAGS
EWGFEHNVIQ LHQVLGVKPD AAGSSGVPVR QWWRS
//
