ID B9XJE4_PEDPL Unreviewed; 2137 AA.
AC B9XJE4;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:EEF60005.1};
GN ORFNames=Cflav_PD3064 {ECO:0000313|EMBL:EEF60005.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF60005.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF60005.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF60005.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:EEF60005.1}.
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DR EMBL; ABOX02000021; EEF60005.1; -; Genomic_DNA.
DR RefSeq; WP_007415937.1; NZ_ABOX02000021.1.
DR STRING; 320771.Cflav_PD3064; -.
DR OrthoDB; 174240at2; -.
DR Proteomes; UP000003688; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd12116; A_NRPS_Ta1_like; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003688};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..434
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 915..997
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2058..2133
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1050..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2137 AA; 233491 MW; A08927BDE693EE83 CRC64;
MTESSLEGIA IIGMAGRFPG AANIPEFWKN LVNGVESITT FTEAELAASG MDVTELRKSP
GYVASRGVLK DAEYFDANFF GMNPKEAEVT DPQQRLFLEA SWEALEDAGY DAGRFTEVIG
VYAGMGNSSY LWNNVQPRPD LVDSVGEMVA MMGNEKDFLA SRVAFKLNLK GPAISVNTAC
STSLVAVCQA CHSLLNYQCD LALAGGISIT FPQKRIFHFQ EGGIVSPDGH CRAFDAQAQG
TVSSDGLGIV VLKRLAEALQ DGDQIYAVIR GVGLNNDGSS KGSFSAPSVD GQADAITQAQ
TFAGFDPATI SYVEAHGTGT PLGDPIEITG LTQAFRTGTD QKQFCAIGSV KTNIGHLDTA
AGVAGLIKTA LALKNKQIPP SLHYARANPR IDFENSPFYV NSTLTEWKAG ATPRRAGVSS
FGLGGTNAHV VLEEAPVTEP SSPSRECQLL VLSAKTDSAL NAATSSLAAC LEANPLLNVA
NAAFTLQTGR AVLNHRRALV CRNGADAAAA LKLLDSKRVF TQHSEVKDAP VVFMFPGQGA
QYVNMGSELY RTEPVFRDEV DACSKVLQPL IGLDLRQVLF PQPEQVQSAE ELLIQTRITQ
PALFVIEYAL AKLWMSWGIK PQAMIGHSVG EYVAGCIAGV FTLQEALVLV ASRAHLVQAQ
PGGSMLAVRL PEKDVLPMLG SELSIAAINS PSLCVVSGPY SAIEQFEAAL KEKGIAGKRL
NTSHAFHSSM MDPVIGPFTE LLKKVLLKEP AIPYVSNATA KWITTAQAVD PHYWAAHVRQ
AVRFADGVAE LLRNPQAILL EVGPGTTLTN LARQHPAKSS EQSVVASLTG TKGQEIPSML
NALGRLWLAG ASVDWNGFYQ QEKRHRVTLP TYPFERKRFY AEPARRVRTQ IALEITSNAD
ETEIRAAESP ADITAATLTR KDRIIGQLLS QLQELSGANL TGLAPSTSFA ELGYDSLFLA
QLSQNLQKKY GVKVTFRQLS EQFSTLDTLA AYLDSQMPAD ASPTLQPVAA RTSFDQKAIS
QDRSWQTLLK AKQAQLVALT KEVEMLQRMG SVQPASPTST SEESKAQGDL RTTFTEPGIA
TPVTLPLTAG QLELWLGTQW GEDASRAMNH SFSIHLRGST NLKALRETIQ EMVDRHDALR
MTFQPDGSAQ RTQPSLLLEV PLSDFSALAE TERNHELQAT EKEQSDRSFD LLNGPLLRVQ
IIKLSEDHHV LLLASHHLIM DGWSISVVFH ELKTIYSAKI QDVSAKLEPA MQFRNYVQWE
KSRDNSSATA NSEAYWLSRF ASPPAAIELP TTRPRPPVKT YKAAHQSVKF DPALYQTLKQ
ACVREGCTLF AYLFASINVW LHRLSGQTDL VVGVPAAGQI AVGEVHPGNK FLVGHCVNLL
PIRSQCAGEM TFKDYLREVK RLVLDAHEHQ QFTFANLVSK LNLPRDTSRM PLVSVTFNLN
RAAAGFHMEG VESQIISLPK GFNIFDLTVD VIDSDKDITI DCRFNTDLFD AQTLGTWLNH
WKTLLTATMA DAAKPVSSIP ILNASDCKQI LQDWNDTRQD YPRNQCVHQL VEAAAAETPN
AAAVVFDGKC LTYQELNRRA NRLAHYLKRN GVGPDVLVGL CVERSLEMVI GLLGILKAGG
AYLPLDPEYP MERVAFILQD AKAPVLLTQQ SLLRKLPVIA PSTDGTSQVQ NRAVFCLDPD
LSAIPERNEE NPVCATTQEN LAYVLYTSGS TGQPKGVQIP HRALVNFLTS TQQEPGMKAS
DVLLAVTTLS FDIAGLELWL PLTVGAKVVI ARSAAALDGK QLIRLLAQCH ATVMQATPVT
WRMLLEAGWA GNPKLNILCG GEVWSEDLVK QLLPKCASLW NMYGPTETTI WSAVDRIQSP
ETPVIGRPMA NTQFYVLGPE MQPVAVGVPG ELHIGGEGLA RGYHKREQLT AEKFIKDPFN
AEPNARLYKT GDLVRYRRDG KIEFLSRIDN QVKIRGYRIE LGEIETILRQ HPYVRDCVLA
ARNGPAGEKR LIGYVVLRPS PVSITSELRS FLKERLPDYM VPSVFVTLEA LPLTPNGKVD
RKALPEPGAK SETDNFVAPE TSTQKALAEI WCEILKLKRI GIHDNFFELG GDSLIATQLM
ARLAELLEIE ITMRDIFEVP TIAAMSDWLE KITVEMA
//
