ID   FABM_STRR6              Reviewed;         261 AA.
AC   Q8DR19;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase;
DE            EC=5.3.3.14;
GN   Name=fabM; Synonyms=phaB; OrderedLocusNames=spr0375;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND GENE NAME.
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=12237320; DOI=10.1074/jbc.m208920200;
RA   Marrakchi H., Choi K.H., Rock C.O.;
RT   "A new mechanism for anaerobic unsaturated fatty acid formation in
RT   Streptococcus pneumoniae.";
RL   J. Biol. Chem. 277:44809-44816(2002).
CC   -!- FUNCTION: Catalyzes the isomerization of trans-2-decenoyl-ACP to cis-3-
CC       decenoyl-ACP. Most active with 10-carbon enoyl-ACP. Can also use 12-
CC       carbon enoyl-ACP as substrate, but not 14- and 16-carbon enoyl-ACP.
CC       {ECO:0000269|PubMed:12237320}.
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         Evidence={ECO:0000269|PubMed:12237320};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000269|PubMed:12237320}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12237320}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AE007317; AAK99179.1; -; Genomic_DNA.
DR   PIR; G97918; G97918.
DR   RefSeq; NP_357969.1; NC_003098.1.
DR   RefSeq; WP_000400072.1; NC_003098.1.
DR   AlphaFoldDB; Q8DR19; -.
DR   SMR; Q8DR19; -.
DR   STRING; 171101.spr0375; -.
DR   EnsemblBacteria; AAK99179; AAK99179; spr0375.
DR   GeneID; 60233333; -.
DR   KEGG; spr:spr0375; -.
DR   PATRIC; fig|171101.6.peg.416; -.
DR   eggNOG; COG1024; Bacteria.
DR   HOGENOM; CLU_009834_7_2_9; -.
DR   OMA; SCDMVVC; -.
DR   BioCyc; MetaCyc:MON-19310; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR   GO; GO:0034017; F:trans-2-decenoyl-acyl-carrier-protein isomerase activity; IDA:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Fatty acid metabolism; Isomerase; Lipid metabolism; Reference proteome.
FT   CHAIN           1..261
FT                   /note="Trans-2-decenoyl-[acyl-carrier-protein] isomerase"
FT                   /id="PRO_0000419023"
SQ   SEQUENCE   261 AA;  28735 MW;  BDA3BECB60D5AF2B CRC64;
     MEHIIYQLEE DLAILTLNRP EVANGFHIPM CEEILEALTL AEENPAVHFI LINANGKVFS
     VGGDLVEMKR AVDEDDIPSL TKIAELVNTI SYKIKQIAKP VLMEVDGAVA GAAANMAVAA
     DFCLATDKAK FIQAFVGVGL APDAGGIHLL SRSIGVTRAA QLAMTGEALT AEKALEWGLV
     YRVSEAEKLE KTREQLLKKL RRASSNSYAA IKKLVWESQF KDWQGYATLE LNLQKSLAQT
     EDFKEGVRAH SERRRPKFIG K