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Database: UniProt
Entry: A3WBK1_9SPHN
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ID   A3WBK1_9SPHN            Unreviewed;       311 AA.
AC   A3WBK1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|ARBA:ARBA00018953, ECO:0000256|PIRNR:PIRNR000446};
DE            EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258, ECO:0000256|PIRNR:PIRNR000446};
GN   ORFNames=NAP1_06560 {ECO:0000313|EMBL:EAQ30418.1};
OS   Erythrobacter sp. NAP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ30418.1, ECO:0000313|Proteomes:UP000002995};
RN   [1] {ECO:0000313|EMBL:EAQ30418.1, ECO:0000313|Proteomes:UP000002995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAP1 {ECO:0000313|EMBL:EAQ30418.1,
RC   ECO:0000313|Proteomes:UP000002995};
RX   PubMed=21952547; DOI=10.1128/JB.05845-11;
RA   Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA   Falkowski P.G.;
RT   "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT   sp. Strain NAP1.";
RL   J. Bacteriol. 193:5881-5882(2011).
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         ECO:0000256|PIRNR:PIRNR000446};
CC   -!- SIMILARITY: Belongs to the fabD family.
CC       {ECO:0000256|PIRNR:PIRNR000446}.
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:EAQ30418.1}.
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DR   EMBL; AAMW01000001; EAQ30418.1; -; Genomic_DNA.
DR   RefSeq; WP_007164448.1; NZ_CH672390.1.
DR   AlphaFoldDB; A3WBK1; -.
DR   STRING; 237727.NAP1_06560; -.
DR   eggNOG; COG0331; Bacteria.
DR   HOGENOM; CLU_030558_0_1_5; -.
DR   OrthoDB; 9808564at2; -.
DR   Proteomes; UP000002995; Unassembled WGS sequence.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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; IPR024925; Malonyl_CoA-ACP_transAc.
DR   InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR000327; POU_dom.
DR   NCBIfam; TIGR00128; fabD; 1.
DR   PANTHER; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   PIRSF; PIRSF000446; Mct; 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.
DR   PROSITE; PS51179; POU_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR000446};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002995};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          296..311
FT                   /note="POU-specific"
FT                   /evidence="ECO:0000259|PROSITE:PS51179"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT   ACT_SITE        203
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ   SEQUENCE   311 AA;  32461 MW;  E975692D6954E39F CRC64;
     MIAFVFPGQG SQKVGMGTEL AAASAAAREV FEEVDEALGM KLSAIMRDGP EDQLTLTENA
     QPAIMANAIA TLRVLEDDFG VKLAETGSCV AGHSLGEYSA LCAVGAFDLA TTARLLKLRG
     SAMQAAVPVG EGGMAALLGA DVEKAAALAA AASEQDVCEV ANDNDPTQVV ISGHKSAIDR
     AIAMAKDHGI KRGIALPVSA PFHCSLMQPA ADRMAEALAE TLPGELALPV YANVTATKVS
     DPEEERNLLV EQVTGRVRWR ESIIAMRADG VERFVELGGK VLGPMIGRID KEAATDSLIS
     MEDLEGFAKT L
//
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