ID W5TWH5_9NOCA Unreviewed; 2460 AA.
AC W5TWH5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Polyketide synthase module-containing protein {ECO:0000313|EMBL:AHH21526.1};
GN ORFNames=NONO_c67590 {ECO:0000313|EMBL:AHH21526.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH21526.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH21526.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH21526.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
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DR EMBL; CP006850; AHH21526.1; -; Genomic_DNA.
DR RefSeq; WP_025352828.1; NZ_CP006850.1.
DR STRING; 1415166.NONO_c67590; -.
DR KEGG; nno:NONO_c67590; -.
DR PATRIC; fig|1415166.3.peg.6941; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000019150; Chromosome.
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 GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.30.300.30; -; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001763; Rhodanese-like_dom.
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; 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; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 250..310
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 728..803
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 816..1240
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2343..2418
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2421..2442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2460 AA; 261369 MW; 313C83788867D8C0 CRC64;
MQADCFEPGV IAIAPDFPRG PVQRFLRARE AHPAAGTVER SLAALVTLLH RHGEHAQVVL
GVVVPQGDSF TAMPLLVDAG PEVTAAQIRA RTDRARADLL ATRERFDSDE LIGRLGVATV
FDRHPLFQVA YCELGTGAVE SAAAEDACDT VVGCDLVFVA DRDTGELRCE FDAELFEPET
VRGLLAQWSV LMDSLAAEEE RALGGLPMLA PELADGWGDG PWADRPATTL TALIAERAAT
APDDIAVVSG DTTLTYAELD ERAARVAGYL TTLGVRPRGI VALCVRRSWR VPVLALGIMK
AGAAYLPLDP ADPDARLSSV LADAGVPVVL CDDADIAGRP AFAEGVTAID LTAVWADIEA
AEAGARRTGS PTDLAYVLYT SGSTGRPKGV LIEHAAICNR LLHNEIRIGE TDRVLQKTPL
TFDVSVWDLF YPLVHGACSV IADPDGHRDS RYLVDVVRAQ SITVAHFVPS MLRTWLAEPG
VADCTSLRYV TTSGEALPAD VAAEFHRLLP ETALYNYYGP TEAAVDVTCE RVLPGAAVTL
GRPIENVRTL VLDDAGQVVP VGVPGQLYLA GVCLARGYVD PDDEIGRFVA DRRRGERLYA
TGDRVRRTAD GRLDYLGRTD HQLKLRGLRI EAGEVEAALR AAGKVREAVV TVHGDDPQRR
ELVGYLVGAP DAVLDTDELR AGLRALLPSY MVPTKFVVLD EFPRNSAGKI DRSRLPAPAD
PVPAGAQSTP TALSATIAAV WAEVLGRDIV PDTANFFDLG GNSLLVARVH LVLEQALGTP
IARTDLFRYP TVAALATALA GAVEGRAEEA EDADRSGPFA VIGMAVRVPG AADVDEFWKV
IAEARTTMTE LGDEELLAAG ESAERIAAPN YVRTAAVLDD IAGFDAGCFG FTAREAQVTD
PQQRILLETA VQALEHAGYG GAPQRPRTGV FVGGLPSSYF HRYFADDFTR LPATQHYQIK
VGNEPDFLPT SLAYRLDLRG PAVTVQTACS TSLVAVHLAC QSIARGECEI ALAGGVAIRV
PDRVGYLHQE GMVASPDGHC RAFDERAAGT IFGNGAGVVV LKRLADAVRD GDRVFAVVRG
SAINNDGSAK VGFTAPGVDG QVEVVRRAHR AAGVRAAEIG YAEAHGTATA LGDPMEIAAL
TEAFGGPRAD RCEVGSVKAN IGHLDTAAGI AGFIKTVLAL DHAVLPGLAD LARPSSRIPW
DDTPFRVSAH SRPWPADRPR IATVSAFGIG GTNAHAVLEA APPRPDTPVA DDWTGLFRLS
AHTPEALRAL ARRYLDRLDA DPGLAIQDLC FTTGFGRAHH AHRLAVVTSS VPELRAALTE
YLADAPAATL FSATDSGAGQ GVCLVLGDVP RQGVAEFLAE FHDDPVVLRA MEEVAAAGGD
APGELARQFV LTRIWQSCGL PLDAVIGYGT GETAAAVASG ALDLASAMRT GSAKPAAVQA
PTGNLWLASA MRDTDPLDAV VAAAVASGRG RLLVLGARGD DRARLRLAAD RHGAHTILAA
DGPHEFRRAL LVAAAKLYVG GADICLTPWG PFAAGQRIPL PTYAFQRTRH WVDAPRERRG
TGGAADAGLL PGRRISLPLS EEIRYEREFS CAAPAYVTDH RLFGTAVVPG ASHIAMVLAA
AAEHIDGPYA LRDTLFLNPF AVSDDGSRAA QLVLRPGGQG WDATLCAQEE SAGAAWPELF
RTVVESAVPE PDSDLTEAGR REVLDRCPEE LSGLEFYRDV WVPGLDTGNS FHWIDTIWRG
DNEALCRTTR PAGVATGSEP LHPGLVEAAF QVLNSCWKYD TDALRAQENI YVPFSIDRYY
FSGRRTEGPL WIHARLIGGH EAGDEAFTAR IRMYSATGEL VVAVDGFESR RIGRAQVERA
LARTSADTTY EQQWVRTGDI ADPARPVALL VVDDRADRLR RFATILDQGG IESVTVLADG
GTPAEQGAWP AEIAHAEYRG FVDLRALSAV DDDSADYVRA LANRYAAAVR PLPALAGQRA
RVWWPTRRAQ AVTGDGDVGD PAATGYWGLA TVVRREFPEL QCSTVDLDDD SDGSLRRLVA
EIRSGAPELR IAHRARQRYV ARLRKARPAT DLAIRSDRTY LITGGLRGIG PRVARALAEQ
GAGHLVLVGR TAPDAEVERL LDDIRGAGCS VTVRVSDIAT GSLTDVIADA PWPLGGIVHA
AGVLDDVTLA GSDAARFEPV LAPKVGGLRT LLGILGADTE FVVFFSSLTA TVGAGGQGNY
AAANAYLDGY ASILRTRGVT ATAIAWGPWD EIGMAARLDP AERERARLRG YRPLAPAQGL
RLLLNNLHAA GATVVAAEVE WAKLAAGADP WYGNLAAAVP APAPVSASMR ERVRAGARID
RIALVRELTT GEVKAVLGLD GAHLVDPGQG FTELGMDSLA VVELRSRLQD GFGVALPATF
GFDYPTIDAA AEYLLGAIES EEPDVESEPV APTAEPEPPE DPIAAELALL EAALHSDARW
//
