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FABM_STRMU
ID   FABM_STRMU              Reviewed;         263 AA.
AC   Q8DSN0; E2IPL4; Q2KHJ2;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase;
DE            EC=5.3.3.14;
GN   Name=fabM; OrderedLocusNames=SMU_1746c;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=21741617; DOI=10.1016/j.archoralbio.2011.06.011;
RA   Zhu L., Zhang Z., Liang J.;
RT   "Fatty-acid profiles and expression of the fabM gene in a fluoride-
RT   resistant strain of Streptococcus mutans.";
RL   Arch. Oral Biol. 57:10-14(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=15205416; DOI=10.1128/jb.186.13.4152-4158.2004;
RA   Fozo E.M., Quivey R.G. Jr.;
RT   "The fabM gene product of Streptococcus mutans is responsible for the
RT   synthesis of monounsaturated fatty acids and is necessary for survival at
RT   low pH.";
RL   J. Bacteriol. 186:4152-4158(2004).
CC   -!- FUNCTION: Catalyzes the isomerization of trans-2-decenoyl-ACP to cis-3-
CC       decenoyl-ACP (By similarity). Required for survival at low pH.
CC       {ECO:0000250, ECO:0000269|PubMed:15205416}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP];
CC         Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927,
CC         ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutants do not produce monounsaturated fatty
CC       acids, exhibit reduced glycolytic capability and altered glucose-PTS
CC       activity, and are extremely sensitive to low pH.
CC       {ECO:0000269|PubMed:15205416}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; HM583675; ADK66337.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59379.1; -; Genomic_DNA.
DR   EMBL; BK005411; DAA05501.1; -; Genomic_DNA.
DR   RefSeq; NP_722073.1; NC_004350.2.
DR   RefSeq; WP_002262530.1; NC_004350.2.
DR   AlphaFoldDB; Q8DSN0; -.
DR   SMR; Q8DSN0; -.
DR   STRING; 210007.SMU_1746c; -.
DR   PRIDE; Q8DSN0; -.
DR   EnsemblBacteria; AAN59379; AAN59379; SMU_1746c.
DR   KEGG; smu:SMU_1746c; -.
DR   PATRIC; fig|210007.7.peg.1562; -.
DR   eggNOG; COG1024; Bacteria.
DR   HOGENOM; CLU_009834_7_2_9; -.
DR   OMA; SCDMVVC; -.
DR   PhylomeDB; Q8DSN0; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0034017; F:trans-2-decenoyl-acyl-carrier-protein isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.12.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism; Isomerase; Lipid metabolism; Reference proteome.
FT   CHAIN           1..263
FT                   /note="Trans-2-decenoyl-[acyl-carrier-protein] isomerase"
FT                   /id="PRO_0000419022"
SQ   SEQUENCE   263 AA;  28927 MW;  9A6E426A99F01C6D CRC64;
     MDFKEILYNV DNGVATLTLN RPEVSNGFNI PICEEILKAI DIAKKDDTVQ ILLINANGKV
     FSVGGDLVEM QRAVDADDVQ SLVRIAELVN KISFALKRLP KPVVMSTDGA VAGAAANIAV
     AADFCIASDK TRFIQAFVNV GLAPDAGGLF LLTRAIGITR ATQLAMTGEA LNAEKALEYG
     IVYKVCEPEK LEKITDRVIT RLKRGSVNSY KAIKEMVWQS SFAGWQEYED LELELQKSLA
     FTNDFKEGVR AYTEKRRPKF TGK
 
 
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