位置:首页 > 蛋白库 > MMAA3_MYCTA
MMAA3_MYCTA
ID   MMAA3_MYCTA             Reviewed;         293 AA.
AC   A5U028; O08053; P72027; Q79FX7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Methoxy mycolic acid synthase MmaA3;
DE            EC=2.1.1.-;
DE   AltName: Full=Mycolic acid methyltransferase;
DE            Short=MA-MT;
DE   AltName: Full=S-adenosylmethionine-dependent methyltransferase;
DE            Short=AdoMet-MT;
DE            Short=SAM-MT;
GN   Name=mmaA3; Synonyms=mma2; OrderedLocusNames=MRA_0654;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN OXYGEN-CONTAINING
RP   MYCOLATES BIOSYNTHESIS.
RX   PubMed=8917504; DOI=10.1073/pnas.93.23.12828;
RA   Yuan Y., Barry C.E. III;
RT   "A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic
RT   acids in Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12828-12833(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It
CC       catalyzes the O-methylation of the hydroxy group of the hydroxymycolate
CC       to form a methyl ether. {ECO:0000269|PubMed:8917504}.
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U66108; AAC44618.1; -; Genomic_DNA.
DR   EMBL; CP000611; ABQ72378.1; -; Genomic_DNA.
DR   RefSeq; WP_003403302.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U028; -.
DR   SMR; A5U028; -.
DR   STRING; 419947.MRA_0654; -.
DR   EnsemblBacteria; ABQ72378; ABQ72378; MRA_0654.
DR   GeneID; 45424603; -.
DR   KEGG; mra:MRA_0654; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_3_0_11; -.
DR   OMA; FHRYDDF; -.
DR   OrthoDB; 1518440at2; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0008171; F:O-methyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR003333; Mycolic_cyclopropane_synthase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PIRSF; PIRSF003085; CMAS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..293
FT                   /note="Methoxy mycolic acid synthase MmaA3"
FT                   /id="PRO_0000398364"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000250"
FT   BINDING         39..40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         78..80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         100..105
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  33263 MW;  0897FA680944C63F CRC64;
     MSDNSTGTTK SRSNVDDVQA HYDLSDAFFA LFQDPTRTYS CAYFERDDMT LHEAQVAKLD
     LTLGKLGLEP GMTLLDVGCG WGSVMKRAVE RYDVNVVGLT LSKNQHAYCQ QVLDKVDTNR
     SHRVLLSDWA NFSEPVDRIV TIEAIEHFGF ERYDDFFKFA YNAMPADGVM LLHSITGLHV
     KQVIERGIPL TMEMAKFIRF IVTDIFPGGR LPTIETIEEH VTKAGFTITD IQSLQPHFAR
     TLDLWAEALQ AHKDEAIEIQ SAEVYERYMK YLTGCAKAFR MGYIDCNQFT LAK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024