NPS2_CERS8
ID NPS2_CERS8 Reviewed; 2464 AA.
AC A0A248AFK6; M2PQ94;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Nonribosomal peptide synthase NPS2 {ECO:0000303|PubMed:28842536};
DE Short=NPS2 {ECO:0000303|PubMed:28842536};
DE Short=NRPS 2 {ECO:0000305};
DE EC=6.3.2.- {ECO:0000269|PubMed:28842536};
DE AltName: Full=Type VI siderophore synthetase NPS2 {ECO:0000303|PubMed:28842536};
GN Name=NPS2 {ECO:0000303|PubMed:28842536}; ORFNames=CERSUDRAFT_172109;
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=B;
RX PubMed=28842536; DOI=10.1128/aem.01478-17;
RA Brandenburger E., Gressler M., Leonhardt R., Lackner G., Habel A.,
RA Hertweck C., Brock M., Hoffmeister D.;
RT "A highly conserved basidiomycete peptide synthetase produces a trimeric
RT hydroxamate siderophore.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B;
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- FUNCTION: Nonribosomal peptide synthase; part of the siderophore
CC basidioferrin biosynthetic pathway (PubMed:28842536). The biosynthesis
CC of basidioferrin depends on the hydroxylation of ornithine to N(5)-
CC hydroxyornithine, catalyzed by the monooxygenase SMO1
CC (PubMed:28842536). The second step, the acylation of N(5)-hydroxy-L-
CC ornithine is catalyzed by a not yet identified N-acyltransferase
CC (PubMed:22434909). Finally, assembly of basidioferrin is catalyzed by
CC the nonribosomal peptide synthase (NRPS) NPS2 via amide bond formation
CC between three L-AHO molecules to release the linear L-AHO trimer
CC (PubMed:22434909). N-5-acetyl-N-5-hydroxy-L-ornithine (L-AHO) and N-5-
CC cis-anhydromevalonyl-N-5-hydroxy-L-ornithine (L-AMHO) are accepted as
CC the substrates by the NPS2 adenylation (A) domain, but only L-AHO is
CC trimerized (PubMed:28842536). {ECO:0000269|PubMed:28842536}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:28842536}.
CC -!- INDUCTION: Expression is induced under iron-depleted conditions
CC (PubMed:28842536). {ECO:0000269|PubMed:28842536}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) that releases the newly synthesized peptide
CC from the enzyme (By similarity). Occasionally, methyltransferase
CC domains (responsible for amino acid methylation) are present within the
CC NRP synthetase (By similarity). NPS2 has the following architecture: A-
CC T-C-T-C-T-C (PubMed:28842536). {ECO:0000250|UniProtKB:A0A144KPJ6,
CC ECO:0000305|PubMed:28842536}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EMD38714.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KY287598; AQX36215.1; -; Genomic_DNA.
DR EMBL; KB445795; EMD38714.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A0A248AFK6; -.
DR SMR; A0A248AFK6; -.
DR STRING; 914234.A0A248AFK6; -.
DR EnsemblFungi; EMD38714; EMD38714; CERSUDRAFT_172109.
DR HOGENOM; CLU_000092_0_0_1; -.
DR OrthoDB; 9183at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 3.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 3.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
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 Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF00550; PP-binding; 3.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 3.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 1: Evidence at protein level;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..2464
FT /note="Nonribosomal peptide synthase NPS2"
FT /id="PRO_0000444316"
FT DOMAIN 814..888
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:28842536"
FT DOMAIN 1364..1437
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:28842536"
FT DOMAIN 1917..1993
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:28842536"
FT REGION 275..670
FT /note="Adenylation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28842536"
FT REGION 924..1325
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28842536"
FT REGION 1479..1887
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28842536"
FT REGION 2047..2340
FT /note="Condensation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28842536"
FT MOD_RES 848
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1398
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1954
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2464 AA; 270791 MW; 6B4536C6E36DE686 CRC64;
MSAHTRTDCD HPELPKLATV ISGYRHCDLP DLSSDRFPAS TTYSVSACIK ESLISTQVDV
LDARAPFAVL VATIGRVLGA YCGCTDVILA LTDQDCEDLR TARITWDENT QWADLLHTVL
QSLSGDTSFR ITVPAIREAL GLTEKQAPCL ALVRDAPSSD YDNTDFPLVF NWDISTFTLR
LFTSERHLHP SGADLLASQI ASLLVPALTN PATQVFRLPD LQADLLSIYE KLTFEDRCQA
YSRVPPVRLA TDHLTLRLAS QANDVAVEWY GALADDHHPG TSQPETMTFG EWHRRANQMA
RWLVARGLEK GDKVAVCMKR DTSYHVSLIA VLKAGACYVP IDPELPSERQ SYIACDSGAR
FVLVSSETAS TSIFGDIALE ISSNEARRGI EAESDEELDL ATPDDVSYLL YTSGTTGTPK
GCVLTHRGLS EAVWALSAVC AEVDMEEGHM GNYLSIASVA FDVHLAEIFI PLARGMSIVS
APRSTLLEDL PYFIKELKIS HLGIVPSLIE ATMGSIQEDV ESGGSTTLRY IASGGEKMSD
AILDKWANHP TVRLANFYGP SEVTIGCAAR FMDKTTPRAN IGHPFASVSA FVVDENMNIL
LRGAPGELVV EGPLVGVGYH GRPDLTEKVF LEFPERGAGR WAYRTGDLVR MMPDGTLEVI
GRIDTQIKLR GVRIESEGIS SIVRSAGLPE HTLDVVTILG KHPAIGVEQL VSFIVWDQST
SVAVRKSTKP TVIAPSGNLL TKLSAACERE LASYMRPSHF IPLNFMPLSS NGKNDAKLLT
RVFQELDMDV LGSLMSRGSS TSVGSPNSGR TQLTKAEGQL LEIAKKHVHV PSGAANPNTN
LFRYGLDSMS AVRLAAELRR TFSKVITASD ILKSPSLEQI AKALDASSSS DQEQSPVESF
VQRFSAERMQ DVTEAYDSHV ISAIYPPFPL QEGILYRSVN ADTLYVQHVL LELAPGVSVD
KLRQAWIDVV ISSPILRTVF HFGRDLVQVV LHSDDVSRDI GEDVVHCDDA EAFKALFAER
QSSVASKINQ NVADTSPHRF TIYRSKDNGL VFVGLSIHHA LFDGISLSHI LRNLEKVYLD
EPGYPSAAPE AVLDTIASVN VQTAQDFWVQ HFAGFDWNRM PSRTASAKRA DEKSLTFQIG
LSELQRKASE RRITLQSLLM TAFAHFLAKY MYGHNDVAFG IIRSGRSLPI ADIETTVLPL
LSVLPARVVL SASDVLRNVQ TFNAEVTAYE HIPLGKIQQW VRPGANLFET LFSLSYKDDG
RSSVWRLLES HNPEPDYILA VEVVLDTTED RLTVQVAYTS QDLSSDIVDH LLDNFEGLAL
DLAQGSALNV ETDSAAESGT ALTSSEQTTQ VTDIDAGEID AVDEDLLLRL RKIVANFLQI
SVDLVTEGVS LVALGLDSIR SVGLSRVLRK EGIELASAEI MKLATPRRMA ASAGKKISIP
STTKHKIDAY ASSFARERDR IRAALDAASV SLSPDDEVDV FPVTTLQAGM LSQTVSSAGR
RYVHLFPLRL TNGVDVAKLR DAWAKTVDAL GILRTTFHFV PDLGIWTSAV HSKSPLKWSE
IYLLEDASLL PLLDAVTITD AGCNSPPYQL YLVRSQEVDS QEDCRLIMVL HHALYDGVSI
SKLLDIVGAS YNGEVTQNIV QFTSLLPEIL WQEHLGTSFW VERLKNFHHG LVVPRLPDGS
HSKKSHVASS VLNVSRSEVE KVCRLTAVTT QCVGQYAFAK LLASLTRSTD ILFGHVVSGR
NVSGAEDVIG PVLNTVPCRV RFASSVSNKL LLQAIHDTNV TALSWQHASL RSIQSHLKVE
RLWDCLFVFQ PSQATETSEH KSVWEFDEVE DEDIDIQYGF NLELHETAAG FLLKAACSDR
LMDAEDLGAA LERFGLFLRV LVDDLDASCL NGLPDLTAPT TPHSVSESDF ETDQIVSSWD
EKSSTLRELL STATGIPSSK IQMSMRLLGL GIDSISAIQI ASKARRTGLH LTARDIIQSR
TVGDLVMRAG AEDESEDRAG QALQTAFQIP RQEWSALTPK VKESDVDSVT VATPGMQWFM
GGWQRSGGSR YQHVFGFELS ADVDILKLQK AWDELLTRHA ILRAAFSSSA QGEPRVVIYK
RESMGARWQE EECDDIQDYD EGVASRMRAL ISSPPSSMQE PLTRATLLRS PSRNALIIHL
HHFQYDAWSL QLLLDDLVRL YQGQPPTSSN DHSAILRVAV PDEHTRTEQR SYWQRMLTPN
DPTLILFPKI PGHQARSNSS HNFLMKKSVL TPIADLEARA RALSVSLYVV YLTCWAQVQA
AATSSNSAIF GLWHSGRTGS IDQVECLAAP CLNILPFVVR GFNSTSTMDI ATQIQDDLRE
RTPLVEQSPL TLVDEVMGGT GRPLCNVFVN IVRAAPELHS TQQTIFTPID VPYFIPEAPS
RGKTAMPELK VTGLIQDDII VDIVDVSERG EVAMSIEFSE DTLDVETAEA MILQWVQLVK
ECLA
