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Database: UniProt
Entry: A0A133XFN4_9RHOO
LinkDB: A0A133XFN4_9RHOO
Original site: A0A133XFN4_9RHOO 
ID   A0A133XFN4_9RHOO        Unreviewed;       313 AA.
AC   A0A133XFN4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE            EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN   ORFNames=AT959_17760 {ECO:0000313|EMBL:KXB29770.1};
OS   Dechloromonas denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB29770.1, ECO:0000313|Proteomes:UP000070186};
RN   [1] {ECO:0000313|EMBL:KXB29770.1, ECO:0000313|Proteomes:UP000070186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB29770.1,
RC   ECO:0000313|Proteomes:UP000070186};
RA   Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.;
RT   "Nitrous oxide reduction kinetics distinguish bacteria harboring typical
RT   versus atypical NosZ.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00000936};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXB29770.1}.
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DR   EMBL; LODL01000035; KXB29770.1; -; Genomic_DNA.
DR   RefSeq; WP_066886034.1; NZ_LODL01000035.1.
DR   AlphaFoldDB; A0A133XFN4; -.
DR   STRING; 281362.AT959_17760; -.
DR   Proteomes; UP000070186; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; IPR017554; Malonate_deCOase_MdcHsu.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   NCBIfam; TIGR03131; malonate_mdcH; 1.
DR   PANTHER; PTHR42681:SF6; BLL0263 PROTEIN; 1.
DR   PANTHER; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070186}.
FT   DOMAIN          6..307
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
SQ   SEQUENCE   313 AA;  32437 MW;  ECF89D0363CA180F CRC64;
     MRLALLFSGQ GGQGPAHWQQ VMDGPDAALR DQLRHLLPEL AGPAATTETT AGPGGDAEKL
     AKNSIAQPLI FAQQMLLWGQ LQPRLPRPIC AAGYSLGEMA ACSAAGAFSA SAGLDLCAKR
     AALMDAAVSG EQGMLAVLGL DEALVEGMAA AAGLAVAIRN APRHLVVAGP RPGLLAVAEQ
     FTAAGASRLV QLAVRTPSHT PQLRSAAVDF QKCLDLLPDA RLAFPVLSAI DATPARTARP
     ALDALARQIC TPLDWAACLQ AVAEMQPDAV LEIGPGNALS RLFAELAPNV PVRACDDFRS
     VDGIVRWVES GGR
//
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