ID L8DMX0_9NOCA Unreviewed; 1796 AA.
AC L8DMX0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:CCQ17333.1};
DE Flags: Fragment;
GN ORFNames=RHODMAR_3947 {ECO:0000313|EMBL:CCQ17333.1};
OS Rhodococcus sp. AW25M09.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ17333.1, ECO:0000313|Proteomes:UP000011207};
RN [1] {ECO:0000313|EMBL:CCQ17333.1, ECO:0000313|Proteomes:UP000011207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ17333.1,
RC ECO:0000313|Proteomes:UP000011207};
RA Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA Smalaas A.O., Altermark B.;
RT "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:CCQ17333.1}.
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DR EMBL; CAPS01000109; CCQ17333.1; -; Genomic_DNA.
DR STRING; 1268303.RHODMAR_3947; -.
DR eggNOG; COG1020; Bacteria.
DR OrthoDB; 2472181at2; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000011207; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd17646; A_NRPS_AB3403-like; 1.
DR CDD; cd17643; A_NRPS_Cytc1-like; 1.
DR CDD; cd19540; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 2.
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 PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 625..700
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1699..1774
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1796
FT /evidence="ECO:0000313|EMBL:CCQ17333.1"
SQ SEQUENCE 1796 AA; 194191 MW; 07BC516DA1A72D5D CRC64;
MAVGRRREAA LTVEDLPRLV RSVAAVEPDR VALAHLGTEL TYARLDEEIT TLDTAMGGVL
GPDALVPVVL SNTVPGLIEA TDGGLDAVVS SVVSDAVSVV GDDDSASSPA APEAATLYAL
FADQAERTPE APALVFGGES RTYAEFAESV ERLARVLIER GVGPDSTVGL SIRRSLDLLV
GMYAISAAGG AYVPLDPEHP VDRLTYVLET ARPVLVLTTS EDLPQLPVGT QTLLVDAVDV
TGVTSGRITD ADRLGTLGED DLAYVIFTSG STGRPKGVAV SHRAIVANIS WRQRAYTMTP
ADVVLQKTPF TFDVSVWEFF WPLQIGATLV IAEPDGHRDP AYLARIVAEH GVTVTHFVPS
MLSVYVAEPT AAQANSLRMV FASGEALPAR TVNAFHTISD AELHNLYGPT EAAVDVTYYR
TQQVEDGSVP IGAAVDDTDL YVLDEGLRRS PRGVEGELYL AGVQLARGYL GRTDLTSDRF
VADPFGEPGD RMYRTGDLVR RRTDGLIEYI GRTDFQVKLR GLRIELGEIE QALLAEPEVT
QAAVLVHTDH SQAQLGEQLV GYVVSTEPDI DHDGLADAVR RRMPEYMVPS VFVVLDEFPL
NASGKLDRKA LPAPDLASLV REYRAPGTDT ETVLVAIFET VLGIDRIGVD DDFFVLGGNS
LNATRVIARV NAELGTAVDV RSFFDAPTVA ELAVAVDSAE SVHARPPLVA QQRPERVPLS
LAQQRMWFLN RFDPDSAVNN IPVAIALSGE LDFEALQAAL VDVLDRHESL RTVYPDHDGI
GFQRVLESDA VAVELERATA TEADVPSALL EFALRPFDLA VQLPFRAVLL ETSATDHVLA
FVVHHIAADG FSMGPLTRDV VGAYVARTDG VAPQWTALTV QYADFTLWQR AVLGSEDDPE
SLISAQESYW RHQLGGAPDQ LELPTDRPRP AVATTNGGTH TFEIDARLVR ELEKLGRDHN
ATTFMVVHAA LAVLLAKLAA ADDISIGTPV AGRGDAALDD VVGMFVNTLV LRTEVDPRTS
FDDLLREIRE VDLAAFSHAD VPFERLVDVL APVRSQARHP LFQVMLTFQN LDRTSVELPG
LTIAAVDYEA DLAKFDLQVT LWDSAPAGSE PAGLTVALTY AADLFDETTM VQFGRRFVRV
LDAVAHSPAA PVGDIEVLDN YERVRALDRV RPAATAAAMA SGTVLGDRFD ARVLADPEAE
AVTFEGRSLS YGDLAARSNR LARELIAHGA GPETLVAVAL PRSAELVVAL LAVLKSGAGY
LPIDTTYPAE RLDFVMLDAR PVVLVVDVDN HGTLPASDIP VVVLAETTAS TRSSTPVTDA
DRLRPVREDN TAYVIYTSGS TGVPKGVRIS HRNVTRLLDN TAELYRFDDT DVWTMFHSFA
FDFSVWELWA PLLSGGRVVV VDFFTSRSPE AMVELLVRER VTVLNQTPSA FYQLIDAERR
LDGAAGVLSL RYVIFGGEAL DPARLDRWVA RHGERPILVN MYGITETTVH VSFRELHPST
DRAAASSPVG DAIPGLSVFV LNSRLQPVPP GVVGEMYVAG EQLALGYLDR PDLSAVRFVA
HPYSHHGERI YRTGDLARLT VDGELDYAGR SDSQVQLRGF RIELGEVESV LERHESVLRA
VVEVRTDDRV GDRLVGYVVP EHGSVVESND LAEFAGGFLT GYMVPDAFVV LDALPLTPNG
KLDRRALPVP LFATREFRAP STPVEEIVAQ VFGDVLGVDR VGVDDDFFAL GGNSLVATQV
ASRLSAELRT KVPVRMLFEA SAVGALAVAL ESHVGSGVST PLVAQERRER IPLSLA
//
