ID Q7D502_MYCTO Unreviewed; 427 AA.
AC Q7D502;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:AAK48192.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:AAK48192.1};
GN Name=cfa-2 {ECO:0000313|EMBL:AAK48192.1};
GN OrderedLocusNames=MT3823 {ECO:0000313|EMBL:AAK48192.1};
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331 {ECO:0000313|EMBL:AAK48192.1, ECO:0000313|Proteomes:UP000001020};
RN [1] {ECO:0000313|EMBL:AAK48192.1, ECO:0000313|Proteomes:UP000001020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh {ECO:0000313|Proteomes:UP000001020};
RX PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J., DeBoy R., Dodson R., Gwinn M., Haft D., Hickey E.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M., Salzberg S.L.,
RA Delcher A., Utterback T., Weidman J., Khouri H., Gill J., Mikula A.,
RA Bishai W., Jacobs Jr W.R.Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; AE000516; AAK48192.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7D502; -.
DR SMR; Q7D502; -.
DR KEGG; mtc:MT3823; -.
DR HOGENOM; CLU_026434_6_2_11; -.
DR Proteomes; UP000001020; 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:AAK48192.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001020};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAK48192.1}.
SQ SEQUENCE 427 AA; 47600 MW; 5830E8D70E4822C5 CRC64;
MTTGRLSMAE ILEIFTATGQ HPLKFTAYDG STAGQDDATL GLDLRTPRGA TYLATAPGEL
GLARAYVSGD LQAHGVHPGD PYELLKTLTE RVDFKRPSAR VLANVVRSIG VEHILPIAPP
PQEARPRWRR MANGLLHSKT RDAEAIHHHY DVSNNFYEWV LGPSMTYTCA VFPNAEASLE
QAQENKYRLI FEKLRLEPGD RLLDVGCGWG GMVRYAARRG VRVIGATLSA EQAKWGQKAV
EDEGLSDLAQ VRHSDYRDVA ETGFDAVSSI GLTEHIGVKN YPFYFGFLKS KLRTGGLLLN
HCITRHDNRS TSFAGGFTDR YVFPDGELTG SGRITTEIQQ VGLEVLHEEN FRHHYAMTLR
DWCGNLVEHW DDAVAEVGLP TAKVWGLYMA ASRVAFERNN LQLHHVLATK VDPRGDDSLP
LRPWWQP
//
