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Database: UniProt
Entry: D4H0Q4_DENA2
LinkDB: D4H0Q4_DENA2
Original site: D4H0Q4_DENA2 
ID   D4H0Q4_DENA2            Unreviewed;       372 AA.
AC   D4H0Q4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ADD68567.1};
DE            EC=2.1.1.79 {ECO:0000313|EMBL:ADD68567.1};
GN   OrderedLocusNames=Dacet_1803 {ECO:0000313|EMBL:ADD68567.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD68567.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD68567.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460
RC   {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC       {ECO:0000256|ARBA:ARBA00010815}.
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DR   EMBL; CP001968; ADD68567.1; -; Genomic_DNA.
DR   RefSeq; WP_013011077.1; NC_013943.1.
DR   AlphaFoldDB; D4H0Q4; -.
DR   STRING; 522772.Dacet_1803; -.
DR   PaxDb; 522772-Dacet_1803; -.
DR   KEGG; dap:Dacet_1803; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_6_0_0; -.
DR   InParanoid; D4H0Q4; -.
DR   OrthoDB; 9782855at2; -.
DR   Proteomes; UP000002012; 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:ADD68567.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002012};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADD68567.1}.
FT   ACT_SITE        343
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ   SEQUENCE   372 AA;  43770 MW;  D8AFDC83BE7A1A31 CRC64;
     MSSIDFKTKI EHALSTADIK TKGDRPWDIT IHNDNLFSRV MADGSLGLGE AYIEKWWDCD
     KLDEFFYRIL SVELETQFKS WTDYKEYLRS KLFNLQNRSR AFQIGQKHYD IGNELYKNML
     DERLIYSCGY WSHANNLKEA QESKLDLVCR KLQLKPGMRI LDIGCGWGGA DKFAAENYGV
     EVVGITVSKE QVELGKCICS GLPVNLELKD YRDISEKFDR IFSIGMFEHV GRKNYKEYFE
     VAKRCLKDDE IFLLHTIGRN TTSKGSDPWI SKYIFPNSML PSAKDIAEFS EGQFVIEDWH
     NFGQYYDTTL MEWYRNFNKN WDKLKDKYDE NFYRMWKYYL LSCAGSFRAR KNQVWQIVFS
     PKGIKGGYEP VR
//
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