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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//