HIPS_NEONM
ID HIPS_NEONM Reviewed; 1678 AA.
AC A0A3G9K3K9;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Hispidin synthase {ECO:0000303|PubMed:30478037};
DE Short=HispS {ECO:0000303|PubMed:30478037};
DE EC=2.3.1.- {ECO:0000269|PubMed:30478037};
DE AltName: Full=Fungal bioluminescence cycle protein hips {ECO:0000303|PubMed:30478037};
DE AltName: Full=PKS-NRPS hybrid synthetase hips {ECO:0000303|PubMed:30478037};
GN Name=hisps {ECO:0000303|PubMed:30478037};
OS Neonothopanus nambi (Agaricus nambi).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Omphalotaceae; Neonothopanus.
OX NCBI_TaxID=71958;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, FUNCTION, DOMAIN, CATALYTIC
RP ACTIVITY, PATHWAY, AND BIOTECHNOLOGY.
RX PubMed=30478037; DOI=10.1073/pnas.1803615115;
RA Kotlobay A.A., Sarkisyan K.S., Mokrushina Y.A., Marcet-Houben M.,
RA Serebrovskaya E.O., Markina N.M., Gonzalez Somermeyer L.,
RA Gorokhovatsky A.Y., Vvedensky A., Purtov K.V., Petushkov V.N.,
RA Rodionova N.S., Chepurnyh T.V., Fakhranurova L.I., Guglya E.B.,
RA Ziganshin R., Tsarkova A.S., Kaskova Z.M., Shender V., Abakumov M.,
RA Abakumova T.O., Povolotskaya I.S., Eroshkin F.M., Zaraisky A.G.,
RA Mishin A.S., Dolgov S.V., Mitiouchkina T.Y., Kopantzev E.P.,
RA Waldenmaier H.E., Oliveira A.G., Oba Y., Barsova E., Bogdanova E.A.,
RA Gabaldon T., Stevani C.V., Lukyanov S., Smirnov I.V., Gitelson J.I.,
RA Kondrashov F.A., Yampolsky I.V.;
RT "Genetically encodable bioluminescent system from fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:12728-12732(2018).
CC -!- FUNCTION: PKS-NRPS hybrid synthetase; part of the gene cluster that
CC mediates the fungal bioluminescence cycle (PubMed:30478037). Performs
CC the biosynthesis of hispidin from caffeic acid by two cycles of
CC addition of malonyl units followed by lactonization (PubMed:30478037).
CC The fungal bioluminescence cycle begins with the hispidin synthetase
CC that catalyzes the formation of hispidin which is further hydroxylated
CC by the hispidin-3-hydroxylase, yielding the fungal luciferin 3-
CC hydroxyhispidin. The luciferase then produces an endoperoxide as a
CC high-energy intermediate with decomposition that yields oxyluciferin
CC (also known as caffeoylpyruvate) and light emission. Oxyluciferin can
CC be recycled to caffeic acid by caffeoylpyruvate hydrolase
CC (PubMed:30478037) (Probable). {ECO:0000269|PubMed:30478037,
CC ECO:0000305|PubMed:30478037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeate + ATP + H(+) + 2 malonyl-CoA = AMP + 2 CO2 + 2
CC CoA + diphosphate + hispidin; Xref=Rhea:RHEA:71123,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57770, ChEBI:CHEBI:190288, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:30478037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71124;
CC Evidence={ECO:0000269|PubMed:30478037};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30478037}.
CC -!- DOMAIN: The architecture of hips is the following one: adenylation (A),
CC phosphopantetheine-binding/thiolation (T), beta-ketoacyl synthase (KS)
CC and malonyl-CoA:ACP transacylase (MAT). Hips homologs in bioluminescent
CC species lack two domains, the ketoreductase (KR) and the dehydratase
CC (DH) domains. {ECO:0000305|PubMed:30478037}.
CC -!- BIOTECHNOLOGY: The availability of a complete eukaryotic luciferin
CC biosynthesis pathway provides several applications in biomedicine and
CC bioengineering. {ECO:0000269|PubMed:30478037}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
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DR EMBL; LC435355; BBH43485.1; -; mRNA.
DR SMR; A0A3G9K3K9; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 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; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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 Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 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; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..1678
FT /note="Hispidin synthase"
FT /id="PRO_0000455704"
FT DOMAIN 586..661
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1597..1672
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 33..453
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30478037"
FT REGION 686..1111
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30478037"
FT REGION 1201..1499
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30478037"
FT MOD_RES 620
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1632
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1678 AA; 180756 MW; 665A86328C20F389 CRC64;
MNSSKNPPST LLDVFLDTAR NLDTALRNVL ECGEHRWSYR ELDTVSSALA QHLRYTVGLS
PTVAVISENH PYILALMLAV WKLGGTFAPI DVHSPAELVA GMLNIVSPSC LVIPSSDVTN
QTLACDLNIP VVAFHPHQST IPELNKKYLT DSQISPDLPF SDPNRPALYL FTSSATSRSN
LKCVPLTHTF ILRNSLSKRA WCKRMRPETD FDGIRVLGWA PWSHVLAHMQ DIGPLTLLNA
GCYVFATTPS TYPTELKDDR DLISCAANAI MYKGVKSFAC LPFVLGGLKA LCESEPSVKA
HLQVEERAQL LKSLQHMEIL ECGGAMLEAS VASWAIENCI PISIGIGMTE TGGALFAGPV
QAIKTGFSSE DKFIEDATYL LVKDDHESHA EEDINEGELV VKSKMLPRGY LGYSDPSFSV
DDAGWVTFRT GDRYSVTPDG KFSWLGRNTD FIQMTSGETL DPRPIESSLC ESSLISRACV
IGDKFLNGPA AAVCAIIELE PTAVEKGQAH SREIARVFAP INRDLPPPLR IAWSHVLVLQ
PSEKIPMTKK GTIFRKKIEQ VFGSALGGSS GDNSQATADA GVVRRDELSN TVKHIISRVL
GVSDDELLWT LSFAELGMTS ALATRIANEL NEVLVGVNLP INACYIHVDL PSLSNAVYAK
LAHLKLPDRT PEPRQAPVEN SGGKEIVVVG QAFRLPGSIN DVASLRDAFL ARQASSIITE
IPSDRWDHAS FYPKDIRFNK AGLVDIANYD HSFFGLTATE ALYLSPTMRL ALEVSFEALE
NANIPVSQLK GSQTAVYVAT TDDGFETLLN AEAGYDAYTR FYGTGRAAST ASGRISCLLD
VHGPSITVDT ACSGGAVCID QAIDYLQSSS AADTAIICAS NTHCWPGSFR FLSAQGMVSP
GGRCATFTTD ADGYVPSEGA VAFILKTREA AMRDKDTILA TIKATQISHN GRSQGLVAPN
VNSQADLHRS LLQKAGLSPA DIRFIEAHGT GTSLGDLSEI QAINDAYTSS QPRTTGPLIV
SASKTVIGHT EPAGPLVGML SVLNSFKEGA VPGLAHLTAD NLNPSLDCSS VPLLIPYQPV
HLAAPKPHRA AVRSYGFSGT LGGIVLEAPD EERLEEELPN DKPMLFVVSA KTHTALIEYL
GRYLEFLLQA NPQDFCDICY TSCVGREHYR YRYACVANDM EDLIGQLQKR LGSKVPPKPS
YKRGALAFAF SGQGTQFRGM ATELAKAYSG FRKIVSDLAK RASELSGHAI DRFLLAYDIG
AENVAPDSEA DQICIFVYQC SVLRWLQTMG IRPSAVIGHS LGEISASVAA GALSLDSALD
LVISRARLLR SSASAPAGMA AMSASQDEVV ELIGKLDLDK ANSLSVSVIN GPQNTVVSGS
SAAIESIVAL AKGRKIKASA LNINQAFHSP YVDSAVPGLR AWSEKHISSA RPLQIPLYST
LLGAQISEGE MLNPDHWVDH ARKPVQFAQA ATTMKESFTG VIIDIGPQVV AWSLLLSNGL
TSVTALAAKR GRSQQVAFLS ALADLYQDYG VVPDFVGLYA QQEDASRLKK TDILTYPFQR
GEETLSSGSS TPTLENTDLD SGKELLMGPT RGLLRADDLR DSIVSSVKDV LELKSNEDLD
LSESLNALGM DSIMFAQLRK RIGEGLGLNV PMVFLSDAFS IGEMVSNLVE QAEASEDN
