NCSB_STRCZ
ID NCSB_STRCZ Reviewed; 1753 AA.
AC Q84HC6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Neocarzinostatin naphthoate synthase {ECO:0000303|PubMed:15147895};
DE Short=NNS {ECO:0000303|PubMed:15147895};
DE EC=2.3.1.237 {ECO:0000269|PubMed:15147895};
DE AltName: Full=Naphthoic acid synthase {ECO:0000305};
GN Name=ncsB {ECO:0000303|PubMed:15797213};
OS Streptomyces carzinostaticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1897;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 15944 / E-793 / F-51;
RX PubMed=15797213; DOI=10.1016/j.chembiol.2004.12.013;
RA Liu W., Nonaka K., Nie L., Zhang J., Christenson S.D., Bae J.,
RA Van Lanen S.G., Zazopoulos E., Farnet C.M., Yang C.F., Shen B.;
RT "The neocarzinostatin biosynthetic gene cluster from Streptomyces
RT carzinostaticus ATCC 15944 involving two iterative type I polyketide
RT synthases.";
RL Chem. Biol. 12:293-302(2005).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15944 / E-793 / F-51;
RX PubMed=15147895; DOI=10.1016/j.febslet.2004.04.033;
RA Sthapit B., Oh T.J., Lamichhane R., Liou K., Lee H.C., Kim C.G.,
RA Sohng J.K.;
RT "Neocarzinostatin naphthoate synthase: an unique iterative type I PKS from
RT neocarzinostatin producer Streptomyces carzinostaticus.";
RL FEBS Lett. 566:201-206(2004).
CC -!- FUNCTION: Iterative type I polyketide synthase that catalyzes the
CC synthesis of the naphthoic acid moiety during the biosynthesis of the
CC neocarzinostatin (NCS) chromophore. {ECO:0000269|PubMed:15147895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 6 H(+) + 5 malonyl-CoA + 2 NADPH = 2-hydroxy-5-
CC methyl-1-naphthoate + 5 CO2 + 6 CoA + 3 H2O + 2 NADP(+);
CC Xref=Rhea:RHEA:42840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:82757; EC=2.3.1.237;
CC Evidence={ECO:0000269|PubMed:15147895};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:15797213}.
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DR EMBL; AY117439; AAM77986.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84HC6; -.
DR SMR; Q84HC6; -.
DR KEGG; ag:AAM77986; -.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; NADP; Phosphopantetheine; Phosphoprotein;
KW Transferase.
FT CHAIN 1..1753
FT /note="Neocarzinostatin naphthoate synthase"
FT /id="PRO_0000449572"
FT DOMAIN 1659..1736
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1696
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1753 AA; 187220 MW; 26DD3002CAB6CEDB CRC64;
MSCRYAPDLD SPDKFWDFLV NGRSTVGDMP DKRWEPYASG SPQATAAMRD TVRRGAFLDD
IEGFDAEFFG ISPREADFLD PQQRFMLELA WEALADAGVP PLTLRNTDTG VYAAANSNDY
GRRLLEDIPR TGAYAVNGTT LYGIANRVSY FLDLHGPSMA VDTACAGALT ALHLARQSLL
TGETPLAIVG GLNIMSTPSL NVALNDAGAM SPDGRSKAFD EDADGYGRGE GAGVLVLKRL
SDARRDNDPV HAVIRGSGVF QDGRSDGMMA PDGDAQEHML RQAYHRAGVD PATVDYVEAH
GTGTPTGDRE EITALAKVFG AGRSPHAPCL IGSVKPNVGH VEGGSGITGV IKTVLALRNE
LIPPTLHDRP RTDVDWDAWG VRLVGQVQEW PSCGRPRRAG VSSYGVGGTI SHVILEESPV
PAATSSADAS TGVRTPALFP LSAASEAGLR ALAGEAAGWV ASRPDTPLPS VGHTLTQRRS
HLAQRAAVVA DSAEQLVDRL REVAEGRNGP GIVSARTSAG RADDAVWVFS GHGAQWSGMG
RRLLASEPVF AATLDALDEV FREELGWTPR EAVTEGGPWT AAHVQALTFA VQIGLADVWR
SKGLRPGAVI GHSVGEIAAA VVAGSLDRDE AARFACRRAA ALQRLDGRGA MVMVGLPFEE
AALRLGDRRD VEAAISAGPH STVLSGDRSA VLRVAEEWQA SEVWTRTVDS DIAFHSVHVD
EVTGDIESAA RLLTPRPPTV PLYTTALSDP RSRAPRDSGY WAANLRKPVR FTEAVRAAAE
DGHRLFLEVS SHPVVAHSVS ETLLDLGIED AAVAGTLRRD TDEVESLLEN LAELHCHGVA
VDWARHHTDG ELVGLPAAVW QHRPYWIFPE TTADAGLGRG HDPASHSLLG GRMTVSGSPT
RQVWQTRLDM DSRPYPQSHG LVGVEVTPAA SIINTFAAAV EEDGPSALTD IVLRTPLAVE
PPRVVQVVRE GRSLSLATRV AEDADADGSE WITHTTAAVT PGVRPAGGRL DTEAIRSRLP
EGSLTRADEM FERMGVEGYA FPWDLEELRH DDHEQLAVLQ IEPSPAQRAT SWAHVIDGAL
TISAMVVSPG DATVLWMSRS IDQVTWSGEP PARLTVHSTR SLRSPHDTVD VRVADERGDV
VCEVVGLRFA AVEHIGAAVL PSELVHEIVW RPWDPEDHEG AEDAPVEQVI LVGDPEATVP
LAEQLESAGM TCVQVGDSPE TGLRPDLFAR PGAVVVAPAL AGSDTAPEEE AERVSWLLVR
TVQRVAEIRA DVTGDAPAQR VWCVTSDVRR ARDERSVAHG PLWGLARIVA GDHPELWGGA
VDIGPSADGI GARLVALLDG AAGTEDVISL TGEGAEVARL SRIDRSADGT PLQCSPSGTV
LITGGLGALG LEVARWLVDR GARRLVLVSR RALPNRTEWP AVTDAETRRR IDGVLALEAL
GVTVRVLALD ITDVDQVSAA LAPEALGLPP VRGVVHAAGV VNNALVDKVD LEGLREVLAP
KVRGAMVLHR LFPPGDLDFF VLFSSCGQFA RLSGQASYAA ANSFLDTLAS HRNAGEHTET
VSLGWTAWRG LGMSSNIDTT MFEANSRGLE AVSATEAFGA WSFGDRFQSD YQAILRVVPT
PVHTPRLPVF RDLPVSGETD GPTGDQLFTT TLEGLPEQEA RERITADVRE QVAGVLNFDP
SEVEVKRPLV ELGVDSVMTV ALRVRLQRRY GLELPPTILW AKPTVAALSE HVCDSLRWDG
EEHGDLAAPT AAA
