ID B9XAZ0_PEDPL Unreviewed; 2088 AA.
AC B9XAZ0;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:EEF63175.1};
GN ORFNames=Cflav_PD5810 {ECO:0000313|EMBL:EEF63175.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF63175.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF63175.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF63175.1,
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:EEF63175.1}.
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DR EMBL; ABOX02000002; EEF63175.1; -; Genomic_DNA.
DR STRING; 320771.Cflav_PD5810; -.
DR OrthoDB; 174240at2; -.
DR Proteomes; UP000003688; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 3.40.50.1820; alpha/beta hydrolase; 1.
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; IPR029058; AB_hydrolase.
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; 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; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 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; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
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; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000003688};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..104
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 591..669
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2040..2088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2071..2088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2088 AA; 232034 MW; CEEFEF58B45F8881 CRC64;
MAQAFGDAGG KSKFCAIGSV KSNIGHLDTA AGVAGLIKAV LALKNKQLPP SLHYTKPNPK
IDFENSPFFV NTQLTDWNPG GIPRRAGVSS FGLGGTNAHV VLEEPPTMPA SSASREWQLL
LLSAKTKSAL NDGTANLTAH FKANPGLKLA DVAYTLQVGR GVFGHRRMLV CRNAADAIKT
LESGDSKRVF TQRSALKDVP VFFLFPGQGA QYVSMGADLY RTEPVFKEEV DRCRKLLQPQ
LELDLHQILF PQPEQADLAK ELLVQTRTTQ PALFVVEYAL ARLWMSWGIK PKAMIGHSVG
EYVAACLAGV FTLEEGLRLV ASRARLVQAQ PGGVMLAVRL SEDELQSLQV DDLSIGAVNA
ANLCVVSGPT GQIEKLEKEL DARNIGNRRL STSHAFHSTM MEPVVSPFLE LLKKVTFKAP
TIPYVSNVTG KWITPAEATD PVYWARHVRK TVRFAEGVTK LLEDSQAILL EVGPGKTLTT
LVLQHAARSP DQMVISSMMP GKDEGQEMLN ALGKLWLAGA TVDWPGFYQQ ESRCRVALPT
YAFERSRFWI EPPAVNTRQL AALANPMREV ATVYEVARSA LTIEESRNGI TRSSRLEHAL
KGLFEEISGI QICHSSRSEA FVELGFYSLL LAQASQFIQK RFGIEVTFRQ LQEELSTLKD
LAQYLDVRLP AETPAVGQGK VEEVEIPPAS TGSESQTSSE PTIFPLTEGQ TELWLAAQLG
ADASRAFNQN FLLHLRGQLR QEFLMQALQE VVNRHDALRT TFLPDGKEQQ IAAHLEIEVP
FVDLSSIAEP TRDQKIRELL KEEDEFTFDL AKGPLFRAKI IKVSTEYHML VISSHHIVMD
GWSMGVVFNE VSRIYSAKLE GKAGLLAPAM QFKEYVEWQQ GTEACKKSAE AEAYWLRQYE
TVPTNLELPA DNARPLNKTY KAGTECLVIS SALYKTLKEA TVEQRCTLFT YLLASFNAWL
YRLSGQEDIA IGVPTAGQIA AANHGHSGNR MLLGHCVNLL PFRSRCNGAI AFKDYLKEVK
RVVLEGYEHQ HLTYGRLVNK LNLPRDTSRL PLISMTFNVV QVTNGVHFSG LESEIGLLTK
SCNFFDITFD LMDSEKDLLI ECRFNLDLFG PGTIKKWLKH WKTMLEAAAA NPAQQICAIP
LLDEAERKQI LCDWNDTDKD YPKSKCLHHL IEAQVERTPK AVAVQFESSQ LTYDELNKKA
NRLAHHLKRL GVGPETLVGL CVDRSLEMVV GLLAILKAGG AYVPLDPHYP KERLAFILHD
CRTPVLLTQQ RLLESLPKLI PESETSSNAK TPTVICLDSD LLTVEQGDER NPKTTVSAEN
AIYVIFTSGS TGQPKGVLIS HRSFINFLIG MQQEPGLEKD DVILAVTTLS FDPAGLELWL
PLVVGAKVVI AKSDVAMDAK RLSKQLAACG ATLLQATPAT WQLLLDSGWT GSPNLKILCG
GEAWSNEMAG QLLPRCRSLW NMYGPTETTV WSAATRVEKA EVPLIGKCIA NMQYHVLDSQ
LQPVPIGVPG ELHIGGDGLA RGYLNREKLT GERFIPNPFK ADPKSRLYKS GDLVRYREDG
RIEFLGRMDN QVKIRGHRIE LGEIESTLRK HAAVRNVVVA AQELAPGDKR LVAYLVLEES
ETVTTAALRQ FVKGQLPEYM IPSAFMVLEK FPLTPNGKVD RKALPLPDSR RTSKSSVAPR
DPLELQLAQI WEKIFNMRDS IAMILSWRHS LLAIRLLLKS RNLPQNLPLV TLFQAPTIEQ
LAGVLRQQGW ESPWLSLVPI KADGAKPPFY CVHGVGGNIL EYMDLAKYMD ADQPFYGLQA
IGLNGKRPWH KSVEEMASHY VEEIKAFQPR GPYYIGGSSF GGLVAFEMAQ QLKAKGEEVA
LLAFFDTRAP GYPRYLANVS AWKLKLNQLA HRVALHWGNF RAARGVEKIT YIKTKAQRWY
RSQIWSFNRM RRRWKEKFES IFWPKAIKEA QKKGLQAACV YVPSKYDGSA TLFRATGQIK
GIYPDPTLGW SELIGKGLEI YDTPGHHGAI VREPRARVLA EQLKESLRKT QAAVMLRREH
VNSKKPHANS NRNGQTQEPA VPEEKEVGQI LITPSGTTNA EELASCQA
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