ID E3HKG1_ACHXA Unreviewed; 420 AA.
AC E3HKG1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase 2 {ECO:0000313|EMBL:ADP18116.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:ADP18116.1};
GN Name=cfa2 {ECO:0000313|EMBL:ADP18116.1};
GN OrderedLocusNames=AXYL_04803 {ECO:0000313|EMBL:ADP18116.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP18116.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP18116.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP18116.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CP002287; ADP18116.1; -; Genomic_DNA.
DR AlphaFoldDB; E3HKG1; -.
DR STRING; 762376.AXYL_04803; -.
DR KEGG; axy:AXYL_04803; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_6_2_4; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000006876; 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; 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 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:ADP18116.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADP18116.1}.
FT ACT_SITE 373
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 420 AA; 46733 MW; DBE996C282AA5AF6 CRC64;
MNPLLSVVER KLQALPVPVQ LVLPDGAVLG PPEPRVRFVT HDKTALAHLA EGAVGVLGQD
YVEGRIDIEG NMRDVMAAAS ALLPGSPVDA ARGGWLTELV RKVVSVWRHS VERDARQIEF
HYDLSDDFYA LWLDPRRVYS CAYYREPGMT LAQAQEAKLD HICRKLRLRE GERFLDVGAG
WGGLLLWAAE NYGVDATGIT LSRNQHAHVS KLIQEKGLAG RVRMELLDYR KLDESAPYDK
IASVGMFEHV GRAQLEGYFA KLRRLLKPGG LIMNHGITAA GVYNAELGNG MGEFIEKYIF
PGGELTHVSV VLETLTNGGL EEVDVENLRP HYARTLWAWS DALEARLSEA ARILGGEQGE
RSLRAYRLYL AGCAMGFEHG WIALHQILGQ HPATGRADEL DNPADQAYPW RRDYMYVKNG
//
