ID A0A2T0T369_9BACT Unreviewed; 2273 AA.
AC A0A2T0T369;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:PRY40079.1};
GN ORFNames=CLV58_107173 {ECO:0000313|EMBL:PRY40079.1};
OS Spirosoma oryzae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1469603 {ECO:0000313|EMBL:PRY40079.1, ECO:0000313|Proteomes:UP000238375};
RN [1] {ECO:0000313|EMBL:PRY40079.1, ECO:0000313|Proteomes:UP000238375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28354 {ECO:0000313|EMBL:PRY40079.1,
RC ECO:0000313|Proteomes:UP000238375};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRY40079.1}.
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DR EMBL; PVTE01000007; PRY40079.1; -; Genomic_DNA.
DR OrthoDB; 4317020at2; -.
DR Proteomes; UP000238375; 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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 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; 1.10.1200.10; ACP-like; 2.
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; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major 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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
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; IPR042099; ANL_N_sf.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; PF00202; Aminotran_3; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 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; 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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 525..599
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 619..1046
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1529..1607
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 501..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2273 AA; 245578 MW; 2519B5489EA3CA15 CRC64;
MPDQRAISTE GVLPDFGYVQ QLVADAMGRT NPDTPAIRAF GQQKTYRQLD EQSGLLSQAI
LRAAPEAERV GISCTRTVEM VVGVLAILKA GKAYLPLDPA YPEARLQQLI ADSQVQVCLA
TAVDEALFTN LGLQVLRSDE SHTGPVRPVT QQSETACVLY TSGSTGKPKG VCLTHRGLVN
MLTNQIRRWA DQPGLQTLQF CHLSFDASFQ EIFVPLLTGG TVHLIDDSYR LNAGRLLDYI
EQEHISRVFL PYVVLQYLTE AAVADSRFPA QLQEVITGGE LLKITPAIAR FFEALPDCTL
MNVYGPTEAS VWVTENRLRG NAQSWPQLPS IGRVVAGCEV VIIDEQLTVV PDGEVGEIGI
CGVCLADGYL NQPERTADAF VDWQHPRLGP TKLYRTGDLA RLLPDGTFDF HGRRDTQVKI
RGNRVELGEI EVLLAQQPAV QQAVVVARED IPGHKRLVAY VVASPADFSV PALRAVLAER
LPDFMLPTYY VRLDDLPRTT SGKVDKAQLP PPDHGRPDLT TLYRPARTAL EKQIVGLWEE
WLQLDPVGCD DNFFELGGNS LLAQQTVAAL EQRGFTVPIT KLYQHPTAAG LAAFMQPAAN
ARPQQTTPEP TSRRPATADD AIAVIGMSGR FPGARTIDEL WTVLTEGRET TRFFTDAELD
ASIPATLRTD PGYVKARGVI DGADQFDARF FGLTPAIAQV MDPQQRIFLE IAYEALESTG
HLPELYGGRV GVFAGCGNNT YYLNNVLPNS AVVAQVGSFQ AMTVNEKDYI ASRTAYQLNL
NGPAVSVYSA CSTSLLAIAQ AVQSLRSGQC EVALAGGASI TAPVNSGHLY QEGAMFSRDG
HTRSFNADST GTVFSDGAGV VLLKRLDDAR RDGDTIYAVI KGVGVNNDGG NKGSFTAPNA
DGQAGSIRMA LADAQVDPAT IRYVEAHGTA TPVGDPIEIE GLTAAFGPQT RQQYCAIGSI
KSNMGHLTQA AGVAGVIKTV LSLYHRQIPA SINYEKPNPT IDFASSPFYV NATLRDWVQD
EAGLPRRAGV SSFGVGGTNV HVVLEEAAVE SREATVDAPD TTTPARPVQL LTWSAKSAQS
RDTYGGQLAD QLRQPNAPAL ADAAFTLQTT RPTYTHRQFA LATTPDELSG ALTSTANART
LSRVPGDVVF LFPGQGAQFL NMGRALYEHE ATFRQAIDDC AGHLLPYLGA DIRRVLYPDT
VSSEAEQQLR NTLYTQAALF VTEYALARLW MSWGIEPSIL CGHSVGEFVA AHLAGVFTLP
DVLRLVAARG RLVSEQPRGS MLSVRVGIEK LRSLVPDTLS VAAINSRHLC VVAGLDEDIA
DFARLLDEQE IPNRPLATSH AFHSAMMDPV VTRFADIVKT IPLSRPQRPI VSTVTGTFLT
DAQATDPGYW ATHLRATVRF ADALDTLFGL DEPLLLEVGP GRTVATLARQ QATDQTMTAL
AGLATQADTK TTYESVLTTL GQLYLHGLPI NWQAFYAGRA TRRVSLPTYA FDRRRCWVNA
PIPATVTTST NERSINTQPI DIPVTTPPMR TTALIDKIYQ LLEDASGIEM AGTSPDTNFL
ELGFDSLLLT QMAITLRNEF GTPITFRQLT ADLDSPKALA AFLDQQLPAE QYQPTPAAAP
VAQPVSQPVP VAAATVAAPV AIPMMPPAAP MPVMAAPAMV PVAMPGGDSA LGLIAQQLQL
LARQVALMQG VAPQPVAVQP APVPPVVQPV PTTPAPQPTS VAAAPAAAAP AKPVTVSMPT
TGTSDLTPEE QIEHKKPFGA TAKIEKHSHE LTTVQRQFLD RLTKQYNQKT AGSKAYAQQH
RSQMADPRVV SGFRPVTKEI VYPIVVNRSA GSRLWDVDGN EYIDVLNGFG SNMFGYQPDF
IKQALHEQIE KGFEVGPQHE LAGEVSQLVC ELTGSERVAL CNTGSEAVLG AMRVARTITG
RSLIVAFSGS YHGIVDEVLV RGSKKLKTFP AASGIMGNVV QNMLILDYGT DESLRIIRER
ADELAAVLVE PIQSRRPEFV PIEFLKELRS ITASSGSALI FDEVITGFRM HLGGAQALLG
IRADMATYGK VAGAGMSIGI IGGKRSFMDA LDGGFWQYGD ASVPEVGVTY FAGTFVRHPL
ALAAAKASML HLREQGAGLQ QALTRKTTYL ADTLNAYLTE RQLPMFIAHF GSLWKLKYTD
DLPYSELLFT LLRQKGIHVW DGFPCFMTEA HTDEEVETVI TAFRQSVDEM IEATFFPKKA
GSNKPAVHEG VTAYSSEPPV AGARLGRDPA GNPAWFLPDP NRPGAYLQVD LTI
//
