ID A0A090VLP3_9FLAO Unreviewed; 1279 AA.
AC A0A090VLP3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000313|EMBL:GAL64249.1};
DE EC=2.3.1.39 {ECO:0000313|EMBL:GAL64249.1};
GN ORFNames=JCM19300_875 {ECO:0000313|EMBL:GAL64249.1};
OS Algibacter lectus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Algibacter.
OX NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL64249.1, ECO:0000313|Proteomes:UP000029644};
RN [1] {ECO:0000313|EMBL:GAL64249.1, ECO:0000313|Proteomes:UP000029644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19300 {ECO:0000313|EMBL:GAL64249.1,
RC ECO:0000313|Proteomes:UP000029644};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus Strains
RT SS8 and NR4.";
RL Genome Announc. 2:e01168-14(2014).
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:GAL64249.1}.
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DR EMBL; BBNQ01000017; GAL64249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090VLP3; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000029644; Unassembled WGS sequence.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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 Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:GAL64249.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000029644};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAL64249.1}.
FT DOMAIN 1..100
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 587..662
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 759..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 141235 MW; 61AC8351161B9F1A CRC64;
MAFGKQDVNK YCAIGSIKSN MGHLTAAAGV AGMIKTILAL KHKQIPASLG FEKPNPSIDF
ENSPFYVNNK LNAWESDGLR KAGISSFGVG GTNVHIVVEE YENEQKVSSA SRSLQVLPWS
AKTQNSLQGY QSELGNYLKT NTDFSLADVA HSLVNTRDSF ANRGFIIAEN TEDAFHKLLL
LDDNKNIKTH LLNITSSELA FLFPGQGAQY LQMGKSLYTE EKVFKEAVDK CADLLKSYIK
LDIRQIIYPE ENSEEAELKL KDTKYTQPAL FVVEYALSQL WMSWGIKPTL FCGHSVGEFV
AAHLAGIFTL EDALHLITMR GKLVSELPGG SMLSVRSNVE LVKNIIPKTL SIAAINSDRL
IVVSGPDKEI ESFSKVLDVE NIANKLLLTS HAFHSTMMNP VLDTFETEVK KITLSVPRLP
IVSTVTGDWL TDAEATSSEY WTNHLRATVN FSGAMETVLK LEDPLLLEVG PGRALTTLSM
QKTGLKSLVS IASLSFPKEN ETAHHSVLHA LGTLWLHGVK PNWNSFYSEQ TRQKLLLPSY
VFDRKPCWVE PLSIELDANK QINNIVNTED QFIDLVRNTE YKFMRKPILL NKISEIIEEN
SGVEIEANDF NHSFLELGLD SLVLTQMAIT FKNELNTPIT FRQLNDELGS PNLLADYIDK
ILPKEAYAPA PAVSPVQAQA SVNYAAPSTP SPQPVNVVSN PNQNTALGLI AQQLQLLGKQ
MELLQGNDNT VAQTQHAPTP VVQDQKPIIA PIIIDSEGLS EDEKKEHQKP FGASPKIEKK
STGVSSKQKA FLDNLVESYN TKTAGSKAYS QKHRSHMSDP RVVSGFKPET KELVYPIVVE
KSSGNRLWDL DNNEYIDTLN GFGSCLFGHQ PDFIKEALHK QIESGYEVGP QHPLAGEVCE
LLSEFTGHER IALCNTGSEA VLGAMRIART VTGRSLVVAF SGSYHGINDE ALVRGSKKLK
TFPAAAGILS QSVQNVLVLE YGTDESLEII RQRSHELAAV VVEPVQSRRP EFQPIEFLNK
VREITKASET ALVFDEVITG FRMHPGGAQA LFNIKADIAA YGKVIGGGLS IGAIAGSSTW
MDAIDGGFWE YGDESYPEVG VTYFAGTFVR HPLALAASKA SLVFMKEQGP ELQTKLTAMT
ENLVSDLIIE IKKRKLPIEV NYFGSLWRLK FLEEIPYSEL LFVLMREKGI HIWDGFPCFI
TNAYNEQDIN KLKSVFVSCL DELVSAGVFN SNSKNSTSFT SDLNEPPKNG ARLGMDEQGN
PAWFIEDLNV ESGFAKIEL
//
