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Database: UniProt
Entry: H0BUS7_9BURK
LinkDB: H0BUS7_9BURK
Original site: H0BUS7_9BURK 
ID   H0BUS7_9BURK            Unreviewed;       407 AA.
AC   H0BUS7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:EHL23855.1};
GN   ORFNames=KYG_05619 {ECO:0000313|EMBL:EHL23855.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL23855.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL23855.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL23855.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC       {ECO:0000256|ARBA:ARBA00010815}.
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DR   EMBL; AGTS01000049; EHL23855.1; -; Genomic_DNA.
DR   RefSeq; WP_008903842.1; NZ_AGTS01000049.1.
DR   AlphaFoldDB; H0BUS7; -.
DR   STRING; 512030.KYG_05619; -.
DR   PATRIC; fig|512030.4.peg.1093; -.
DR   OrthoDB; 9782855at2; -.
DR   Proteomes; UP000003485; 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:UP000003485};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   ACT_SITE        388
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ   SEQUENCE   407 AA;  45512 MW;  A4E70754889383EE CRC64;
     MNSTTAPRTA VALPAGTPAA ARTALKLLQR LQHGHLTVQL PDGTLQHFGH GNGPSAAITL
     KNWNVCSAAL KSGDIGFAES YIAGDWTTPH LTDLLKLFIA NRQQVEGVIY GTWAGRLLYR
     IKHLLNRNTR ANSQKNIHAH YDLGNAFYEL WLDDTMNYSS AWFEGDAGGD MRAAQHAKVR
     RALRMAGVQA GDRVLEIGCG WGALAEMATT EFGASLTGVT LSTEQLAFAQ KRMAAHGVQA
     KADLRLQDYR DIQDGPYDAI CSIEMVEAVG REYWPTYFQS VNRLLKSGGK ACIQSIVIDD
     SLFERYISST DFIQQYIFPG GCLPCPREFR REGEAAGLRV VDEFAFGQDY AETLKRWRER
     FLAQRTQILQ LGFDQRFMHI WEFYLAYCEA AFAMSNIDLV QYTLVKD
//
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