AZIB_STREG
ID AZIB_STREG Reviewed; 1779 AA.
AC B4XYB8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=5-methyl-1-naphthoate synthase {ECO:0000305};
DE EC=2.3.1.236 {ECO:0000269|PubMed:18635006};
DE AltName: Full=Azinomycin biosynthesis protein B {ECO:0000305};
GN Name=aziB {ECO:0000303|PubMed:18635006};
GN Synonyms=azi26 {ECO:0000312|EMBL:ABY83164.1};
OS Streptomyces sahachiroi.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=285525;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=ATCC 33158 / NBRC 13928 / NRRL 2485;
RX PubMed=18635006; DOI=10.1016/j.chembiol.2008.05.021;
RA Zhao Q., He Q., Ding W., Tang M., Kang Q., Yu Y., Deng W., Zhang Q.,
RA Fang J., Tang G., Liu W.;
RT "Characterization of the azinomycin B biosynthetic gene cluster revealing a
RT different iterative type I polyketide synthase for naphthoate
RT biosynthesis.";
RL Chem. Biol. 15:693-705(2008).
CC -!- FUNCTION: Polyketide synthase that catalyzes the biosynthesis of the
CC bicyclic aromatic compound 5-methyl-1-naphthoate in the biosynthesis of
CC the antitumor antibiotic azinomycin B. {ECO:0000269|PubMed:18635006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 7 H(+) + 5 malonyl-CoA + 3 NADPH = 5-methyl-1-
CC naphthoate + 5 CO2 + 6 CoA + 4 H2O + 3 NADP(+); Xref=Rhea:RHEA:42836,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78251;
CC EC=2.3.1.236; Evidence={ECO:0000269|PubMed:18635006};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000303|PubMed:18635006}.
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DR EMBL; EU240558; ABY83164.1; -; Genomic_DNA.
DR AlphaFoldDB; B4XYB8; -.
DR SMR; B4XYB8; -.
DR KEGG; ag:ABY83164; -.
DR BRENDA; 2.3.1.236; 13388.
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 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..1779
FT /note="5-methyl-1-naphthoate synthase"
FT /id="PRO_0000430810"
FT DOMAIN 1664..1742
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1746..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1702
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1779 AA; 187473 MW; 54CF1EECFDDC9EA1 CRC64;
MAENVQNPPV EPLAVIGMSC RFAPDLDTPG RLWEFLRAGG SAVGEMPDRR WDPYVTDSRT
RDILRTTTRK GSFMRDIEGF DAEFFQITPR EAEYIDPQQR IMLELAWEAL CDAGLPPTSL
AGTDASVYVA ANSNDYGRRL LEDLDRTGAW AVNGTTFYGI ANRISYFLDA HGPSMAVDTA
CAGSLTALHV AGQALHRGET SVAIVGGINI MASPALVVAL DAASATSPDG RSKSFDKAAD
GYGRGEGGGV VVLKRLSDAV RDGDPVHGLV LASGVFQDGR SDGMMAPNGS AQQRMLEEIY
RRSGIDPGTV QYVEAHGTGT QLGDAAEAQA IGNVFGPGRD GDNPLLIGTL KPNVGHVEAA
SGIAGVIKVL LGMRHGELPP SPHEEPDPGL GLEARGLRLV AEPTPWPRGE HGMRAGVSSY
GVGGSIAHAV LQQAPPRPDR TERPAAAATG RPQVFPLSAA SEQGVRGLAG SVAAWLRAHP
ETALDDLAHT FTARRSHLSR RAAVVAGTTE ELLGGLDALA GGEKSPAVAL ASASGFGDGG
AAGPAWVFSG HGAQWSGMGR ELLTTEPVFA QVIDELAPVF SEELGWTPRE AIEAGGPWTV
VRTQAMTFAM QVALAEVWSD LGLRPGAIIG HSVGEIAAAA VAGSLDRAEA ARFACRRARA
LGKIAGRGAM AMVPMAFADV EQRVAGRDAV VAAIAASPLS TVVSGDTAAV EALLADLEAD
GIQARRVNTD VAFHSPHVQE ILDEVRQAAA ALRAGTPRVT LYSTALADPR SDAPREGEYW
ATNLADPVRF HQAVRAALDD GTRVFLEVSS HPVVAHSITE TALDAGVPDA HVAITLRREQ
PEQRTVLANL ARLHSLGTPV TWSYDGDLVD VPAVRWQHKP YWIFPDTAPE QGAGLGHDPQ
THTLIGARTT VASAPVQRVW QTELHMENRP YAQSHKVVGV ETVPASVVLN SFITAATNEG
ERACGLRDIV FRIPLAAHPT RVVQVVLEQD KVRIASRIKR DQESGGVRDD EWLTHTTATV
VHEPEVGARP MEDPDVIRAR CPVSWTWAKV DGIFRTMGVD GYTFPWVVEE LLRGEDEQFS
TITVDHTPKL HPSSWTAVVD AALTASGVLV MDENSNVLRT CSHLESLSFV GPPPPRIHVH
TVRDPRTPDT ISMTVADESG AVVCEARGLR YVKVQDIGSG AVGPRDLVHE LAWEPVEVPA
DAPVPSQALV VGGAAGGPAL VEALTARGVR ARAVPDATAI GDASLTCADV VVVAPEALLP
GEAPEQAARR CAQLLVDAVQ QVAAVPDERR RPRVWALTRE VRAGATEAAL AHAPLWGAGR
IVAGERPDLW GGVIDVAENA VPQQVASLIG ALPHTEDVLS LDSEGVTAAR LRQVARPAER
EPVDCRPDGT YLVTGGLGAL GLEAARHLVE QGARRLVLIG RRGLPSRSRW DQVDDPAVAA
QIAEVVALEA AGATVRVLSL DISDAEATAR ALDPGALDMP PVRGIVHCAG VVSDALVEKT
GAANLDTTMG PKADGAMVLH RLFPAGTLDF FTMFSSCGQL ARLTGQVSYA SANSFLDALA
ALRRSRGETG TTSFAWAQWI GRGMGETTGR ATILEAESRG LGGITVSEAL RSWAYADRFA
LPYAAVMRVM PDHTLPVFSH LSVTDAGAQS ADAGGVDWAT VPAGELPELV LKVTHEQVAA
ELNLAVDDIA IDQPLLELGV DSVLTVALRV RLHRCFAVDL PPTILWSNPT VRALAEFLAA
EVGGATADAE ETDPVAGLPA PQQGSGTAEQ LDAVAAAAG
