ID K8EHP3_9FIRM Unreviewed; 392 AA.
AC K8EHP3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:CCO08156.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:CCO08156.1};
GN ORFNames=DESHY_20025 {ECO:0000313|EMBL:CCO08156.1};
OS Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO08156.1, ECO:0000313|Proteomes:UP000009315};
RN [1] {ECO:0000313|EMBL:CCO08156.1, ECO:0000313|Proteomes:UP000009315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT hydrothermale Lam5(T).";
RL Genome Announc. 1:e00114-e00112(2013).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCO08156.1}.
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DR EMBL; CAOS01000009; CCO08156.1; -; Genomic_DNA.
DR RefSeq; WP_008411403.1; NZ_FQXF01000016.1.
DR AlphaFoldDB; K8EHP3; -.
DR STRING; 1121428.DESHY_20025; -.
DR eggNOG; COG2230; Bacteria.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000009315; Unassembled WGS sequence.
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:CCO08156.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCO08156.1}.
FT ACT_SITE 359
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 392 AA; 45372 MW; 5B6D7BF5D75FE568 CRC64;
MTKERMKGLF ERFKGGNFTV TFWDGETCRY GQGPPVVSFI FHKPLDTTFN LDKPLLSLGE
AYMDGYWDFT GEFTEIIRII EENKELLKPA GLTGKITGFI QSVTAKRQQK QNIEHHYDLG
NDFFSLWLDE TLSYSCAYFK NPDDTLYQAQ INKIDHTLKK LQLKPGERLL DIGCGWGWLV
IRAAQQYGVR ALGITLSDQQ YAAAGRRVKE LGLAGQVEIR LASYQDLSEQ EQQFDKIVSV
GMFEHVGRDN LPRYMEQVNK LLVPGGLSLL HTITGMTEEP VNDWMEKYIF PGGYIPSLRE
IIWLLPLYRF HLLHAESLRL HYAKTLDHWY NNFSRCVAKV REKFDERFVR MWSLYLRGCA
ASFRVSGLDI YQLLFSKGLN NNLPMDYGFI YA
//
