ID D5X5F3_THIK1 Unreviewed; 423 AA.
AC D5X5F3;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ADG31846.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:ADG31846.1};
GN OrderedLocusNames=Tint_2505 {ECO:0000313|EMBL:ADG31846.1};
OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG31846.1};
RN [1] {ECO:0000313|EMBL:ADG31846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 {ECO:0000313|EMBL:ADG31846.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA Heinhorst S., Woyke T.;
RT "Complete sequence of Thiomonas intermedia K12.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CP002021; ADG31846.1; -; Genomic_DNA.
DR AlphaFoldDB; D5X5F3; -.
DR STRING; 75379.Tint_2505; -.
DR KEGG; tin:Tint_2505; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_0_2_4; -.
DR BioCyc; TINT75379:TINT_RS12545-MONOMER; -.
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:SF2; TUBERCULOSTEARIC ACID METHYLTRANSFERASE UFAA1; 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:ADG31846.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADG31846.1}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 423 AA; 47332 MW; 6F028125785A0326 CRC64;
MNASDRSLSP LSLDPTLAAG QTRKPRKPPL AARGVLRLLE RLQIGRLDFH GPDGVWRHFG
QDDNGPHAEV ALHDWAVMGE VLKRGDIAFA EAWMRRAWDT PDLPALLKLL VANREIIARA
LHGSLLGRLP DRIRHLLRRN SRAGSRDNIH AHYDIGNAFY QLWLDPSMTY SSALFSGNPA
QTLEQAQAAK YARVLDQLQL QPGARVLEIG CGWGGLAEVG AQRGLRLDGI TLSAEQLAYA
RARLAQPAPP ARLELCDYRD LDRIAPPDGY DGIASIEMFE AVGEAYWPGF FRTVARQLKP
GARACIQTIT IADDLFDDYR RGTDFIQRYI FPGGMLPSRR AFIAQAKAAG LEVVEELAFG
ADYAHTLALW RERFTAQLEA VKAQGFDDRF LRLWTFYLAY CEAGFSQSTT DVWQFTLRHA
RAH
//
