ID K5BKL3_MYCHD Unreviewed; 283 AA.
AC K5BKL3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Cyclopropane mycolic acid synthase 3 {ECO:0000313|EMBL:EKF25064.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:EKF25064.1};
GN ORFNames=C731_0941 {ECO:0000313|EMBL:EKF25064.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF25064.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF25064.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC {ECO:0000313|Proteomes:UP000006265};
RX PubMed=23209251; DOI=10.1128/JB.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
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:EKF25064.1}.
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DR EMBL; AMRA01000024; EKF25064.1; -; Genomic_DNA.
DR AlphaFoldDB; K5BKL3; -.
DR STRING; 1122247.GCA_000379865_03368; -.
DR PATRIC; fig|1122247.3.peg.903; -.
DR eggNOG; COG2230; Bacteria.
DR OMA; PLKKWPE; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000006265; 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; IPR047672; CMAS_actinobact.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; NF040660; mycolic_MTase; 1.
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:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EKF25064.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006265};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKF25064.1}.
FT ACT_SITE 265
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
FT BINDING 29..30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 64..72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 90..95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 119..120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
SQ SEQUENCE 283 AA; 32679 MW; 64A14E89EE5409C1 CRC64;
MKVAYEDVQA HYDTSNEFFG LFQDPTRTYS CAYFERDDMT LEEAQIAKID LALGKLDLRP
GMTLLDVGCG WGSVMKRAIE TYDVNVIGLT LSRNQRALGQ EILDAIDTQR SRQVLLKGWE
EFDQPVDRIV SIEAFEAWPK SKYKAFFDTC YRIMPDDGRM VLQTIMGHPL RRWPDLGIPI
TISDLKFMRF ILKEIFPGGA VPCDEDVIEY SQNSGFTVEH FESMTPHYVR TLDTWASQLE
AHKDEAIAVT NQETYDRYMR YLTGCSDFFQ RNVSYVGQFT LVK
//