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Database: UniProt
Entry: L8JU28_9BACT
LinkDB: L8JU28_9BACT
Original site: L8JU28_9BACT 
ID   L8JU28_9BACT            Unreviewed;      1853 AA.
AC   L8JU28;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000313|EMBL:ELR72270.1};
GN   ORFNames=C900_01685 {ECO:0000313|EMBL:ELR72270.1};
OS   Fulvivirga imtechensis AK7.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Fulvivirga.
OX   NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR72270.1, ECO:0000313|Proteomes:UP000011135};
RN   [1] {ECO:0000313|EMBL:ELR72270.1, ECO:0000313|Proteomes:UP000011135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK7 {ECO:0000313|EMBL:ELR72270.1,
RC   ECO:0000313|Proteomes:UP000011135};
RA   Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Fulvivirga imtechensis AK7.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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:ELR72270.1}.
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DR   EMBL; AMZN01000025; ELR72270.1; -; Genomic_DNA.
DR   RefSeq; WP_009579120.1; NZ_AMZN01000025.1.
DR   STRING; 1237149.C900_01685; -.
DR   PATRIC; fig|1237149.3.peg.1638; -.
DR   eggNOG; COG3321; Bacteria.
DR   OrthoDB; 4317020at2; -.
DR   Proteomes; UP000011135; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011135};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..435
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1747..1822
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1853 AA;  208122 MW;  76CFF943D684575B CRC64;
     METTKQNIKD TDIAIIGMAG KFPGADNLDQ FWDNLKQGVI SIKRFSDEDL IENEVNKQDL
     QHPNYIRAKG TLSDIEYFDG EFFDYTGREA EILDPQIRLL TELSWHALED AGYVPEKYNG
     NIGVYTGVTN NLYWQLKMIA SGKITNNETL SVAIYSEKDH VSTRISYKLN LTGPSFTVET
     QCSTSLVAFH LACQGIINGE CDMAIAGGAS INLPNKAGYI YQEGSIHSKD GVCRAFDENA
     NGTVFSDGAG LVVVKNARKA IADGDNIYAI VKGSAVNNDG LEKAGFTAPS VSGQKKVITH
     AYEKAGVNPE TITYIETHGT GTAIGDPIEI EALTRAFNTN KRGYCRIGSL KPNVGHMDNA
     AGIGNVIKAT LAIKNKQIPP SVNYNKPNPK IKFEETPFVV NTQLVDWEEN QSYPRRAGVS
     SYGVGGTNAH VLLEEYISQD QVEVNNDGLY LIPFSAKSEY SFNALKANLQ RYLEGYPGSL
     SDIAYTLQTG RRDLSYRHVI LGNSEDEVLK KLKVATPSSA KKTEDIRTIF LFPGQGAQYV
     NMGRGLYEQC KPFRRALDQC FEIYAQITNE DLREIVFGDL REEGSTINET KNVQPLIFSF
     EFALARVLME AGIKPDYMIG HSIGEYTAAC ISGVLSLQDA MKLVIKRGEL IQSLPKGSMM
     AIMMEPEDLK PILSRDISIA AINSTGITVV SGEDKAIDEL DTTLKRQGVE GRKLHTSHAF
     HSHMMDPAID KFEQMFKEVD INEPQIGYMS NLTGKPIQGE EIKKPSYWSA HLRNTVLFKD
     NIENLPDKGN SIFIEVGPGN VLSSFVKRFS SESRNYAIYN TIRHPQEKVS DTEVFYNVLG
     KIWQKGLAVN WNKVFDNSAR RKVSVPVYPF ERKKHWVKGN VYQIAQGAAD GTVKYKDSEM
     LYNRRLYRPT WVETALEPQT LDTNSKSWIV FAEDGDLVSQ HILTQTKELS KYALIVNNGD
     EYKRLKNGYV INHENKHDYK QLFNELKAGI NDKEINILHF WSLNFDSELD IHSSKSREFQ
     AKGLISILFI VQTISAIFPK NKVNIKIFTN NIHHISYKDI LNPLNATVLG AITTVPLEYK
     NIDLWGLDLD LKHLERPVLA NDAINAMITH NSNDKILALR NDKLFTRTFE SMPFKYELEL
     QNIIKDNGVY LVTGGLGGIG VELATYLSKT AKVKLALTGR SEFPDRNKWD KLVKSGGNIA
     DRIRRIQEIE SNGAEVMLVK ADVADKSSME SCVNQVQAKF GPVNGVLHCA GVAGGNIIPT
     LEPNLIYDTM NSKVFGTLIL DELLQQGNNN LDFMVLCSSI SSITGTFGQM SYTASNSFLD
     AYTHYKNAQG KRNVICFNWD IWQEVGMATK AMKELNREDD IRVEPGDLLE HPLFVGQANM
     EQKRVYLSHL SPQLHWMIDE HRILNQPVLP GATYVEMLGF IASNEFATKQ FKIHNLNLYT
     PFVVDENTEK SLYTVLKEES GVYHFSIRQK YNSEKDGLCA KGTLEALGLE KRDTVNIAQI
     LQRCNAQTID NAKNELNKDT SFLELGKRWT CLKSIHLGEE EGVAAIEMPD EYSDDFTDYN
     YHPAMLDIAF NYFAAWKIGQ NEYLPFSFKN MKVYKAIPQK LYSYVKQNGN LQGLKETISF
     NVNLVDEFGE LIISIEEYIL KKVYSDTVKG GGGIGKLYDQ KREDSKDALL EEGIKSEEGT
     KIFDTILSNY LLTGSSDYSQ VVVSNNDLRA ILESGEDTDA YSYFKSNKSD NDQPFTGRPE
     LSELYEAPIN DRQEKLCEFF QNYLRIDKVG VNDNFFELGI SSLDVAEIKI GIEEGFQIEL
     PVAVIFENPN IKALANFIAQ ELGEDEKKEE IIDRTDQVNE GRKLLQRRLL TSD
//
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