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
//