ID A0A077MBT3_9MICO Unreviewed; 434 AA.
AC A0A077MBT3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative cyclopropane-fatty-acyl-phospholipid synthase UfaA1 (Cyclopropane fatty acid synthase) (CFA synthase) {ECO:0000313|EMBL:CCI53310.1};
GN ORFNames=BN13_350008 {ECO:0000313|EMBL:CCI53310.1};
OS Tetrasphaera jenkinsii Ben 74.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI53310.1, ECO:0000313|Proteomes:UP000035720};
RN [1] {ECO:0000313|EMBL:CCI53310.1, ECO:0000313|Proteomes:UP000035720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI53310.1,
RC ECO:0000313|Proteomes:UP000035720};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(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:CCI53310.1}.
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DR EMBL; CAJC01000145; CCI53310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077MBT3; -.
DR STRING; 1193518.BN13_350008; -.
DR Proteomes; UP000035720; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000035720};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT ACT_SITE 413
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 434 AA; 47580 MW; ADBA52F490C66038 CRC64;
MAVVASPPAK SAPGQEIGNR AMSTYQDARL LPLGNGSQTT RAAIAKAIVR RVVERVDVRV
RLADGQTIGA GGPDSPVLEL RSPEAFYRRL AQHPKIGIGD GYVTGEWQPA PGTDLADALV
PFAARLDALI PRPLLALRGL ADSALPTHHR GTIENARTNI SAHYDLSNAL FAAFLDPSMT
YSSALFAGAG QWRQQPLQEA QWRKIDRALD EAGVAPGSRV LEIGTGWGEL AIRAAARGAE
VVSITLSAEQ QQLARERASA AGLSDRVDIR LQDYRDVAGE FDAIVSIEMI EAVGEEFWPD
YFRAIDRLLA PGGRAVIQAI LMDHQRLLAT RHSHGWIQEY IFPGGLIPSL RAIDLVTGTH
THLRRRATFS FGPHYAETLR RWRERFLATY DAIAGPGFDD QFKRRWEFYL AYCEAGFAAG
YLDVAQLTFG KDQS
//
