ID A0A086ZD80_9BIFI Unreviewed; 1132 AA.
AC A0A086ZD80;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=ACP S-malonyltransferase {ECO:0000313|EMBL:KFI44480.1};
DE EC=1.3.1.9 {ECO:0000313|EMBL:KFI44480.1};
DE EC=2.3.1.38 {ECO:0000313|EMBL:KFI44480.1};
DE EC=2.3.1.39 {ECO:0000313|EMBL:KFI44480.1};
DE EC=2.3.1.86 {ECO:0000313|EMBL:KFI44480.1};
DE EC=3.1.2.14 {ECO:0000313|EMBL:KFI44480.1};
DE EC=4.2.1.59 {ECO:0000313|EMBL:KFI44480.1};
DE Flags: Fragment;
GN ORFNames=BBIA_2622 {ECO:0000313|EMBL:KFI44480.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI44480.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI44480.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI44480.1,
RC ECO:0000313|Proteomes:UP000029108};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|ARBA:ARBA00005254}.
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:KFI44480.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JGYN01000048; KFI44480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086ZD80; -.
DR eggNOG; COG0304; Bacteria.
DR eggNOG; COG0331; Bacteria.
DR eggNOG; COG2030; Bacteria.
DR eggNOG; COG4981; Bacteria.
DR Proteomes; UP000029108; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.2430; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 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; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18094; DNA_pol_B_N; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:KFI44480.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFI44480.1};
KW Lyase {ECO:0000313|EMBL:KFI44480.1}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KFI44480.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029108};
KW Transferase {ECO:0000313|EMBL:KFI44480.1}.
FT DOMAIN 533..924
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 980..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1132
FT /evidence="ECO:0000313|EMBL:KFI44480.1"
SQ SEQUENCE 1132 AA; 121206 MW; BB51DD6892CF4B4A CRC64;
MAWFPVLVRE YPKPMPFVPV IDHDLLRWWG QDQLWQSEDA RYSADSVRAI PGPISVAGIT
TVDEPIADIL GRFESAAIAR VQDERGVADT ADTASAERAG FAALGESRDA EDFIRKSPNI
SWVGHITDNP AYGTALGDRN YEIRAFDAAA GKYDLDIHLD TYWDDDPDGG LSKHAVRDIV
IPLVVDGAEP GRVPVVDRER LIPDVYAMLA ATAGIGNTAI TGDKLAAMPE ITAAEGKPFG
EARARYTLSA NLGFDHETAT AGQLPQDLVA SRIAPDALVG PAWPAIYAAL GSVMVDGYPV
IEGLLNAVHL DHLIELETDE EHLLHHVGET VALTSWAEDY FESASGRVVT IHVTHTAADG
TLLARETERF AIRGRVYSDA LPETAPDNGD WTALHDAEIA PTVRRVLRRV TVTAPADMTA
FARTSGDFNP IHTSVRGARI SGLKAPLVHG MWLSAVAQHV AQAVDAKGAH YEIAGWTYNM
YGMVQLNDRV EITVERVGKV RHGGLALEVT CRIDGAIVSR GTAVTRAPIS AFVYPGQGIQ
KQGMVLDERA KSAAARDVWE RADRLTRSKL GFSILALVRD NPKELTANGV TYRHPDGLLN
LTQFTQVALA TVAFAQTARL REAGADIWPS YFAGHSLGEY NALSSFAGVI PLETVLELVF
HRGSTMHHLI PRDAQGRSNY RMGALRPNQF GVGDDGVREY VESVAKASGE FLQIVNYNLA
GAQYAVAGTI AGLKALQADS ARRVAEYGGK PAFMLVPGID VPFHSTLLRK GVPEFRDKLD
ALLPAEIDYR GRLVGRYIPN LVACPFEMTR EFAAKILEVV PSERIRAALD DPAVWDSYAA
DDQKLGRLLL TELLSWQFAS PVRWIETQAL MFGDRTAGGL GVEEYVEVGL GNAPTLANLG
SKTLRLPQFA NRSVAVYNVG RDEGRVYMTD TDSLAPEVDD VPEQAAAPAP SSQFEKLAAA
SAPSAEGAVS HRLTGGASAA TAANSNASTS DRSLSAAPQA GASAVTELGS APSGPVEDLP
FRASDAIGVL MAYSAKVRLD QIGASDTTDT LTNGVSSRRN QLLMDISSEL GVASVDGAAE
ATLTQLAQIV NKAAPNYKPF GPVLSDAIRD RLRALFGAAG VKPRTSASAS PA
//
