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Database: UniProt
Entry: A0A099XNQ1_9FLAO
LinkDB: A0A099XNQ1_9FLAO
Original site: A0A099XNQ1_9FLAO 
ID   A0A099XNQ1_9FLAO        Unreviewed;       295 AA.
AC   A0A099XNQ1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446};
DE            EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446};
GN   ORFNames=PHEL85_2835 {ECO:0000313|EMBL:KGL58571.1};
OS   Polaribacter sp. Hel1_85.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL58571.1, ECO:0000313|Proteomes:UP000029991};
RN   [1] {ECO:0000313|EMBL:KGL58571.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL58571.1};
RA   Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA   Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT   "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT   the North Sea during a spring diatom bloom.";
RL   ISME J. 0:0-0(2014).
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:KGL58571.1}.
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DR   EMBL; JPDS01000003; KGL58571.1; -; Genomic_DNA.
DR   RefSeq; WP_036826581.1; NZ_JPDS01000003.1.
DR   AlphaFoldDB; A0A099XNQ1; -.
DR   STRING; 1250005.PHEL85_2835; -.
DR   eggNOG; COG0331; Bacteria.
DR   OrthoDB; 9805460at2; -.
DR   Proteomes; UP000029991; Unassembled WGS sequence.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
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   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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR000446};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          5..293
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ   SEQUENCE   295 AA;  31137 MW;  DCF348E3BC84971D CRC64;
     MKAYVFPGQG AQFTGMGLDL YEKSPLAQEY FEKANNILGF SITDIMFEGT AEQLKETKVT
     QPAIFLHSVI LAKVLGDSFQ PEMVAGHSLG ELSALVANGV LTFEDGLKLV SKRALAMQKA
     CEAAPSTMAA VLGLADNIVE ETCAEIDGVV VAANYNCPGQ LVISGEIAAV EKACEVLTEK
     GARRALLLPV GGAFHSPMME PAREELAAAI EATEFSEPTC AVYQNVVAKA VTSPDEIKEN
     LIAQLTAPVK WTQCVQAMIA DGGTEFIEVG PGKVLQGLMR KIDRSVAASG AALAE
//
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