ID A0A097R0E9_HAFAL Unreviewed; 310 AA.
AC A0A097R0E9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AT03_07090 {ECO:0000313|EMBL:AIU72180.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU72180.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU72180.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU72180.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the fabD family.
CC {ECO:0000256|PIRNR:PIRNR000446}.
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DR EMBL; CP009706; AIU72180.1; -; Genomic_DNA.
DR RefSeq; WP_025800745.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097R0E9; -.
DR KEGG; hav:AT03_07090; -.
DR PATRIC; fig|1453496.5.peg.1414; -.
DR eggNOG; COG0331; Bacteria.
DR HOGENOM; CLU_030558_4_1_6; -.
DR OrthoDB; 9808564at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000029986; Chromosome.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR024925; Malonyl_CoA-ACP_transAc.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR NCBIfam; TIGR03131; malonate_mdcH; 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 Reference proteome {ECO:0000313|Proteomes:UP000029986};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT DOMAIN 6..292
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 86
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT ACT_SITE 195
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ SEQUENCE 310 AA; 33321 MW; 41189D1D168F6BB2 CRC64;
MKVLFTFPGQ GPQRPAMLHD LPDNALSRSL IEQANTALNE DVLALDSDSA LQRTRAVQLC
LLIAGVAYAR ELQSAGVQAD FVSGLSIGAF PAAVIAGALD FSDAVRLVAL RGELMEKAYP
TGFGLSAIVG LNLNQLEPLI AEVNSADLPV YLANINAEEQ FVIAGSEAAM QQVMALAQAK
GAHKTQRLAV SVPSHCALLL EPAHQLAQAM QNVVLQRPNI AYLSGSTGRV LWQPERIADD
LAFNMSRTVR WHEAMVAAYE REVRLAIEMP PGAVLTGLTR KVMDQGEALS RCQLGLKSVT
DIVARYQKLA
//
