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Database: UniProt
Entry: A0A367RV28_9NOSO
LinkDB: A0A367RV28_9NOSO
Original site: A0A367RV28_9NOSO 
ID   A0A367RV28_9NOSO        Unreviewed;      2477 AA.
AC   A0A367RV28;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Non-ribosomal peptide synthetase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=A6770_38810 {ECO:0000313|EMBL:RCJ39570.1};
OS   Nostoc minutum NIES-26.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1844469 {ECO:0000313|EMBL:RCJ39570.1, ECO:0000313|Proteomes:UP000252107};
RN   [1] {ECO:0000313|Proteomes:UP000252107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tabuchi Yagui T.R.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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:RCJ39570.1}.
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DR   EMBL; LXQD01000072; RCJ39570.1; -; Genomic_DNA.
DR   Proteomes; UP000252107; 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; cd12115; A_NRPS_Sfm_like; 1.
DR   CDD; cd05931; FAAL; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 2.
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; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR040097; FAAL/FAAC.
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; IPR006162; Ppantetheine_attach_site.
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; 2.
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; 2.
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; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252107};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          605..682
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1669..1744
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1767..2194
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   NON_TER         2477
FT                   /evidence="ECO:0000313|EMBL:RCJ39570.1"
SQ   SEQUENCE   2477 AA;  274830 MW;  A392886ED09E213C CRC64;
     MENLFESKNI LESTLIDLLH WRAIQQPKRC AYKFLADGET QTDQLSYQEL DRQACAIATR
     LKSLGASGER ALLLYPPGLE FIAGFFGCLY AGLIAIPAYP PHPNRSMSRI QGIVADAQPK
     VALTTTAIFS KLEQRLLHIP ELKSLCWLES DLVANDQELS WQIPTVSSNT LAYLQYTSGS
     TSIPKGVMLS HKNVLYNSEC IRQAFKLTSD SISISWLPHF HDMGLIDGII QPLYSGFTGF
     LMPSVSFLQK PLRWLQAISR YKATHCGGPN FAYDLCASKI TPEQKQNLDL SNWYSAYNGA
     EPVRPETLEG FAAAFDMCGF RANFFYPCYG LAEATLMVSG GLVGDKSVEC AVEVNALEKN
     QVVKLCHTTN NGKKLVGCGR PWLDTKIVIA QSESQRQCAT EEVGEIWVSG TSVAQGYWQR
     PEQTKETFQA YLADTGEGPF LRTGDLGFIQ DGELFVTGRL KDLLIIRGRN HYPQDIEITV
     EQSHNALRPG CGAVVEVSVE GEQRLLVIQE VERSYLRQLN VEEIASAIRQ SVAQKHELQV
     YAVVLLKTGS IPKTSSGKIQ RHACRIGFET GTLDEVARSV LEQWNELETG AQLSRDEFLA
     MVPEDSQQQL LNYLQQQVSR LLKIAPSQLD SQQPLSQLGL DSLMAVEFKH YLETHLGVTV
     VIADLLQDSS VAQLTTKVLA KMQNSLLQPT SAFVPLSEPA LEYPLSQGQM ALWFLHQLAP
     QSSTYNTFFA ARILSNLDVA ALRQAFQVLS DRHSAIRVTF TISNGQPIQK IQTHLQVVVE
     EIDATNWSQD ELNQQLANSA HHAFNLEQEL PIRVNLFRRG AGEDILLITA HHIAIDFWSL
     EVLLGEISIL YPQMKTGLPK LPKLNWQYAD YVHWQADMLA TDQGEQLWSY WQKQLAGELP
     VLNLPTDRPR SPMQTYQGGV ETFHLQGELV ERIKILTQTE GVTLYMLLLA AFQILLYRYT
     SQEDILVGSP MAGRSRAELS RIVGYFVNPV VLRVNLSQNP TFEEFLAQVR QVVVEALDHQ
     NYPLSLLVKR LQPERDLSYS PLFQVMFVLE KSQRLEDLAG FWWGKNGSQI DLGGLLLESL
     VVEQQVALFD LTLTMLETEG ELVGSWQYNS DLFDANTITR MAEHFQNLLA SIVANPQHHV
     QELSLISTAE QHQLLLEWNH TQSEYPQNQC VHQLFETQVE QTPNAVALVF ENQQLTYREL
     NAQANQLAHY LRGLGVGTET LVGICIERSI EMVVGILGIL KAGGAYVPLD PTYPQERLAL
     MLSDAQLPVL LTSQDLIAGL PSHNALVVYL DRDWQAISQE KQYNPITNTK PTNLAYILYT
     SGSTGQPKGV AVEHLSTVNF LHWVREVYTS EQLAGVLAST SINFDLSVFE LFAPLCRGGL
     VILAENTLHL PTLSAAENVT LLNTVPSVIT ELLRINGIPD GVRTFNLAGE PLSYQLVQQL
     YEHHPNTQVF NLYGPTEATT YATFTLVQKG ESQSPTIGRP LANTQVYILD SLLQPVPIGV
     VGELYIGGVG LARNYLHRPD LTSEKFIPNP FSNQPNARLY KTGDLARYLS DGNIEFLGRR
     DHQVKIRGFR IELGEIEAVL AQHPMVQETV VLVREHSGEQ RLVAYLIPQQ KPLVLNELRY
     FLKQKLPQYM IPSAFVSLDS LPLTPNGKID RRALRNTEIQ PQIAATNVPP QTKTEKLIAA
     VWQELLHLEN VSIYDNFFDM GGHSLLMVQV CSRLKGIFNQ DISIVNIFKY PTINDLAKYF
     TQEESENLAL ELSQKQNFNR NNQDDHNSEI AIIGMSCRFP GAPNIEAFWQ NLRDEIESIS
     FFSDEELLST GVKPELLSHP NYVRSKAVLP DIELFDAAFF GFSPKEAKTI DPQHRLFLEV
     SWEALESAGY NPKPFAGEIG VYAGVGMNTY LLNNLYQNRE LVDSVGEYQL MIGNDKDFLP
     TRISYKLNLT GPSVNVQTAC SSSLVAVHLA CQSLRNNECD MALAGGVSIR VPQLSGYLYQ
     DGMILSSDGH CRAFDAQAQG TVPGNGLGVV VLKRLADAIA DGDCIHAIIK GSAINNDGSV
     KVGYTAPSVD GQAAVIADAQ AIAGVNPETI TYIEAHGTGT VLGDPIEIAA LTQAFQKSTQ
     NQGFCAIGSV KTNIGHLDAA AGIAGLLKTV LALKHKLLPP SLHFQQPNPQ IDFANSPFYV
     NTELCKWETD GIPRRAGVSA FGIGGTNAHI ILEEAEGIQN SKFKIQKQDV TERPLHLLTL
     SAKSEKALEE LTLSYQQYLA NHLEINLADI CFTANVGRSH FDHRLALVAE SSLQLREHLA
     ALASGSTTNE VLMGTSSSHS PEIAFLFTGQ GSQYVGMGQQ LYYTQPTFRA AFDRCDQILQ
     PYLETPLLKA LYPQQTEEKT ENSPLLDQTA YTQPALFALE YALYQLWTSW GITPKTVMGH
     SVGEYVAACV AGVFSLEDGI KLIAARGRLM QALPKDGEMV AVFANENKVR AAIQPYSKDV
     AIAAINAPNN LVISGKS
//
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