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Database: UniProt
Entry: D9W5R5_9ACTN
LinkDB: D9W5R5_9ACTN
Original site: D9W5R5_9ACTN 
ID   D9W5R5_9ACTN            Unreviewed;       492 AA.
AC   D9W5R5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Malonate decarboxylase, epsilon subunit {ECO:0000313|EMBL:EFL20243.1};
DE   Flags: Fragment;
GN   ORFNames=SSNG_07495 {ECO:0000313|EMBL:EFL20243.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL20243.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL20243.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL20243.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; GG657752; EFL20243.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9W5R5; -.
DR   STRING; 253839.SSNG_07495; -.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_554985_0_0_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.50.11460; -; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE   4: Predicted;
FT   DOMAIN          1..289
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFL20243.1"
FT   NON_TER         492
FT                   /evidence="ECO:0000313|EMBL:EFL20243.1"
SQ   SEQUENCE   492 AA;  51795 MW;  B6327BF7926542A9 CRC64;
     GQGAQRPGMG DELYAAFPVY ARAFDAARTA LDAHLDRPLR QVVSGAAELL DRTRYTQAAL
     FALEVALYRL FESWGVRPDF LLGHSVGELA AAHVAGVLTL PDAATLVAAR GRLMDALPEG
     GAMVSVEAAE DEVRALLAAG VDIAAVNGPR AVVVSGPEDA VTRTACLLEA AGHRTKRLNV
     SHAFHSSLME PMLAEFGRIA RTLTFHRPSL PIVSNVTGRT ADPAELATPE YWVRHVRAAV
     RFHDGMRHLE GQGVRRFVEL GPSGVLTAAG RACVNDPDLV LVPALRRDRP EAETVAAALG
     ELFVHGTTPD WTGVFAGQPA HRVDLPTTAF RRTRYWPRPG DTTGRPAAAA QDPAADLQYR
     IEWQPLATPA TTAPDGTWLV AGPCPRELDL VTGALAARGA TPARLDLAPG TGHDRDALTL
     RLLTALPAAD GCAGVLLLPA EAGDPGLDAA LRLHQALGDA GITAPLWCAT RGAVSTGPGD
     RPADPGQAQV WG
//
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