MPBA_MORAP
ID MPBA_MORAP Reviewed; 5541 AA.
AC P0DUV4; A0A7S7ADA4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=Malpibaldin synthetase {ECO:0000303|PubMed:33158886};
DE EC=6.3.2.- {ECO:0000269|PubMed:33158886};
DE AltName: Full=Nonribosomal peptide synthetase mpbA {ECO:0000303|PubMed:33158886};
DE Short=NRPS mpbA {ECO:0000303|PubMed:33158886};
GN Name=mpbA {ECO:0000303|PubMed:33158886};
OS Mortierella alpina (Oleaginous fungus) (Mortierella renispora).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Mortierella.
OX NCBI_TaxID=64518;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, CATALYTIC ACTIVITY,
RP AND INDUCTION.
RX PubMed=33158886; DOI=10.1128/aem.02051-20;
RA Wurlitzer J.M., Stanisic A., Wasmuth I., Jungmann S., Fischer D., Kries H.,
RA Gressler M.;
RT "Bacterial-like nonribosomal peptide synthetases produce cyclopeptides in
RT the zygomycetous fungus Mortierella alpina.";
RL Appl. Environ. Microbiol. 87:0-0(2021).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=30789272; DOI=10.1021/acs.orglett.9b00193;
RA Baldeweg F., Warncke P., Fischer D., Gressler M.;
RT "Fungal Biosurfactants from Mortierella alpina.";
RL Org. Lett. 21:1444-1448(2019).
RN [3]
RP FUNCTION.
RX PubMed=33918813; DOI=10.3390/jof7040285;
RA Koczyk G., Pawlowska J., Muszewska A.;
RT "Terpenoid biosynthesis dominates among secondary metabolite clusters in
RT mucoromycotina genomes.";
RL J. Fungi 7:0-0(2021).
CC -!- FUNCTION: Nonribosomal peptide synthetase that catalyzes the
CC biosynthesis of the hydrophobic cyclopentapeptides malpibaldins,
CC natural products that show biosurfactant activities (PubMed:33158886)
CC (Probable). Module 3 shows promiscuous adenylation (accepting either
CC Trp, Phe or Tyr) leading to the parallel production of multiple
CC products from one NRPS assembly line, including malpibaldin A
CC corresponding to cyclo(-L-Leu-D-Leu-D-Phe-L-Leu-D-Val-), malpibaldin B
CC corresponding to cyclo(-L-Leu-D-Leu-D-Tyr-L-Leu-D-Val-) and malpibaldin
CC C corresponding to cyclo(-Leu-Leu-Trp-Leu-Val-) (PubMed:33158886).
CC {ECO:0000269|PubMed:33158886, ECO:0000305|PubMed:33918813}.
CC -!- INDUCTION: Expression is induced in the presence of fructose.
CC {ECO:0000269|PubMed:33158886}.
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. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Contains
CC bacterial-like dual epimerase/condensation domains allowing the
CC racemization of enzyme-tethered L-amino acids and the subsequent
CC incorporation of D-amino acids into the metabolites. MpbA has the
CC following architecture: C-A-T-E/C-A-T-C-A-T-E/C-A-T-E/C-A-T-TE.
CC {ECO:0000305|PubMed:33158886}.
CC -!- BIOTECHNOLOGY: Mortierella alpina biosurfactants may have an enormous
CC potential for various applications in pharmacy, health care, food,
CC cosmetics, or textiles since they offer a highly biocompatible and
CC biodegradable alternative for synthetic surfactants in formulations.
CC {ECO:0000269|PubMed:30789272}.
CC -!- MISCELLANEOUS: The surprising structural and mechanistic similarity to
CC bacterial nonribosomal peptide synthetases (NRPSs) points to an
CC endobacterial origin of the Mortierella mpcA and mpbA genes that differ
CC from their asco- and basidiomycete counterparts and may have evolved
CC independently. {ECO:0000269|PubMed:33158886}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; MT800759; QOW41314.1; -; Genomic_DNA.
DR SMR; P0DUV4; -.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 4.
DR Gene3D; 3.30.300.30; -; 5.
DR Gene3D; 3.30.559.10; -; 4.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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.
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 InterPro; IPR001031; Thioesterase.
DR Pfam; PF00501; AMP-binding; 5.
DR Pfam; PF13193; AMP-binding_C; 5.
DR Pfam; PF00668; Condensation; 5.
DR Pfam; PF00550; PP-binding; 5.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 5.
DR SUPFAM; SSF47336; SSF47336; 5.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 5.
DR PROSITE; PS00455; AMP_BINDING; 5.
DR PROSITE; PS50075; CARRIER; 5.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 4.
PE 1: Evidence at protein level;
KW Isomerase; Ligase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Repeat.
FT CHAIN 1..5541
FT /note="Malpibaldin synthetase"
FT /id="PRO_0000453667"
FT DOMAIN 901..975
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2001..2075
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3058..3132
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4140..4214
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 5219..5294
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..378
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 401..799
FT /note="Adenylation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 1021..1469
FT /note="Dual epimerase/condensation (E/C) domain 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 1489..1899
FT /note="Adenylation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 2095..2537
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 2557..2956
FT /note="Adenylation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 3182..3616
FT /note="Dual epimerase/condensation (E/C) domain 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 3637..4038
FT /note="Adenylation 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 4260..4695
FT /note="Dual epimerase/condensation (E/C) domain 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 4716..5117
FT /note="Adenylation 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT REGION 5315..5523
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33158886"
FT MOD_RES 936
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2036
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3093
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4175
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 5254
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5541 AA; 608769 MW; FC7FD8A300BDFB65 CRC64;
MGDKRPDGIK SAESHGQPSA PFGAENSEVV QRTLEAVIAQ ATDVIDTASI SLRVVQVENT
GEVNSTILKV TRNKAAECIP SPARSSSPDQ EGDCSSIVTV QRSHECKSFC ATPLTRTAST
ASVASSLSTL RPGSSEKEDD IARDESAKVH ADPWHVALAE AHAPLELFTD RPRHSGLSLA
RAQHTFRIDT PLKQLLASLS VEHKLSFSTT ILVGWSIVLS RLTGQEDILV GLGNVDTPIM
PVRIDLAGDP NTPQLLARVR DTLLVAGASP DLKDKCNTRL LPLFPGETFP SVQAEFYAHG
DQASDKIQNS APASVDIELH LHDAAQDAFA CIRYPTALFN ADTIERHAGY LVAVLMNMVI
NGSQSVATID IISPAEKTLV LKTWNESSSE YPADRCVQRL FEEQVDKSPD AVAIVHENQS
FTYLELDALA DRIAHKLVHA GIKQGDFVTT LLPRSVELVA AQLAVLKVGA AYVPIDPKAP
LDRQVFIVND SASRLLITDI HVETATALDL PLLRIDIAEL QSKEEYSGVI TLTRSSQDAA
YVMYTSGSTG RPKGVMVLHQ GIVRLVMNNG FAPIGPGDRV AFAANPAFDA STFEVWAPLL
NGGCLVVIDS DTSAHPKRLE DALKRYHINT LWLTMTLFNQ YVCSIGPALA KLKYLLCGGE
QGNQETFAAL LKHGGPQNLI NGYGPTEATT FATTYNASRM RNKPDRLPIG RPIGSTYVYV
LDKHGNLAPL GAVGELHIAG AGVAAGYLNR PDLTAEKFLP NPFSKTQGAY MYKSGDLVRY
LPDGNLVFVG RNDDQVKIRG FRIELGEIEA RLVEHDLVRE SVVLALGEGS EKRLVAYVVA
EPTEGLAHTL RSHIEERLPV YMIPAAFVRL GAIPVTANGK IDRRALPEPQ EDAFARQAYE
VPCGETEDAI AAIWSELLGV NQISRHDSFF ALGGHSLLVV KMLDRLHRLG LTVSVRVLFE
SPTLSVLAQD LSKHQAMIIP PNLITLETSK LTPEMLPLID LKQDDIDRII SQVPGGIHNI
QDVYSLAPLQ DGILFHHLLA AEGDPYLLIS HLAFRDRVLV DRYLDAFQKV VDRHDILRTA
VFWDALSTPA QVVLRSAPLS VTEHVLDPAA GPVADKLSQR YNHSKYRMDL TQAPLLRFAL
AEDIDGRWIM AQMMHHLIID HAAIEVMNAE VEAVLEGRED TLSTPPQFRD LVAQVRAGPT
QEEHEHFFAE MLGDIEEPTF PFGLTEVHSN GDEVKEAHMT VPQDLNDRLR AQAKRLGVTL
AALCHTAWAQ VLARTSGQDH VVFGTVLVGG LQGEQSDQSG MGISINTLPF RCDMDDRSVQ
ECVSQIHSRL AALVEHENAS LALAQRCSGV PAGSPLFSAL MNYRHTLMPT SGCDPSDIEF
TAKEERVNYG GIDFLGGQER TNYPFTLSVE DFGQALGLTA QVLQPVDPAD VCRYVQQALS
SLVLALENAP DMAVSDLDVL PLDERTKLLQ LWNATNSPYP DHLCVHALFE QQVKQSPITI
AVEHGDQSIT YAQLNITASH LAYQLSAQGI GHGDRVATYL PRSFELITAQ LAILKIGANY
VPIDPKAPLD RQAYIVSDSG SRLVITDEDT DVPVAIGAPL LRLTSFRKLQ LSTAMDAGWR
AYSGLDSPKT TIERSSLETA YIMYTSGSTG LPKGVMVPHR GIARLVFNNS FTSISSSDRI
VFGANPAFDA STFEVWAPLL NGGRVVIIDA EVLTDSRLLA ETIETRQVTV LFLTPALFNQ
YAESIGQSLA RLRYIISGGE QGNLEAYSAL LRHKGPVQII NAYGPTEATM VATTFTASFD
VSGLDVLPIG RPIGNTQVYV LDQHRHPVPM GVVGELYISG PGVANGYLNR LDLTEDRFFP
DPFTEIHGSR MYKSGDMVRY LPDGNLVYMG RNDDQIKIRG FRVELGEIEA RLVQHSQVRN
AVVVPCGEVD DKRLVAYIAA DPSEHWARTL HNHLASTLPE YMIPSAFVQL DALPMNNNGK
IDRRALPTPD ASAFATENYV SPQGRIECAL AEIWAEVLKV PRVGRHDNFF LLGGHSLLAV
RLMNRISTLG AQLPLSALFA SPTLSSFAQA FKGQLSQDDQ SHNVIPRVSR SEPLELSFSQ
QRLWFLAQME GVSEIYHIPS VLRLRGTLNL EAWQRTLDTL FARHESLRTV FSTVQSQPQI
KILPADLGLP LVHHDLRGEQ DKHASLKLLS AAEAIMPFDL ERGPLIRAQL IQLTDDEHIF
LLTQHHIVSD GWSFGILIRE LRELYIAYRN GLPNPLRPLA IQYPDYAAWQ RCWLNEGRLE
AQSAYWKKTL AEAPVSIELP TDRPRPPQQS FTGASVPVRV DAHVTQALKA LSQKHGATMF
MVVLSAWSAV LSRLSGQDDI VIGSPSANRG HEQVEQLIGF FVNTLALRVD LSGQPNMEQL
LKRVRETTVS AQAHQDLPFE QVVEIAQPPR RMDQTPLFQV LFAWQNNDIE MLRLPDLDVT
VEELSYDIVK FDLELELYED KDEICGCLHY STALFDASTV ARHVGYLEAM LRAMATNISQ
PIETVELLGS TEEELLLQTW NQTEKPFPDD RCIHGLFEDQ VERSPDAIAV VHDDRILTYR
ELNVRADIVA FQLARAGVRP GDSVLTLLSR SINSVVSQIA ILKAGAVYVP MDPKAPADRL
AYMAADSCAR LLVTDECLIV PISIQVPILR LENQPSKNPE RHDIVVISRE TTANDTAYVM
YTSGSTGLPK GVMVSHRAIT RLVVNNRLAH ITSDDRMALS INPTFDPSTF EVWAPLLHGA
QLVILDHDII TDAQCLAEAL DHNDITFLVL PMALFHQFAF VIAPALSRLR YIMCGGEQGS
IEAFSSILQQ GGRVRLINGY GPTEVTTVTT AYVATGSLVS LDRLPIGRPI SNTRVYVLDK
LRRPVPLGAV GELYIGGPGV ATGYLNRPEL TAERFLTDPF SKIEGARMYK SGDLVRYLSD
GNLIFMGRND DQVKIRGFRV ELGEIEERLL EHALVRETVV VVTGEGNGKR LVAYIVSEPT
VQLPVLMREH LGASLPEYMI PTAFVRLETM PLTNNGKVDR RALPEPDSDS FVNKDYEEPQ
GEVEMKLAAI WSELLKVDKI GRQDNFFMLG GHSLLAVQMI GQLRRIGFVM SVRALFETPV
LSVLAASITR GCEVPETPAT PVNLITATTA KITPDLLPLI DLSQDDIDRI TDQIPGGVAN
IQDIYSLSPL QDGILFHHMM ATEDDPYLLT ICTAFRDRDL LERYLDAIQQ IVDRHDILRT
AIVWRNMTTP AQVVLRKAAI SVTELTLDPA NSPIIEQLRK LYDARKHRIE LDVAPLNRYA
VAQDTDGRWI MIQMLHHIVG DHSTLELMDE EIQKIFSGRG ETLAAPQPFR NLIAQVRSGL
TFQEHEEFFS KMLSDIDAPA LPYGLSDVHR EGANVTETQL MLPQKLNDRL RSQARRLGVS
LASLCHLAWA QVIAATSGQY HVVFGTVLFG RMQGGSGADR AMGLFINTLP LRVDVEKGSI
LESVHKVQTD LATLLEHEHA SLALAQRCSS IPSGSPLFSA LLNYRHNDDT FTQSELDSGI
EIIDGHERTN YPFVLSVEDC GTSFGVTVQV VEPYASASVC GYMQQVLQSL ADALEHTPDA
PIQGLKVIPA EEHDLLIHSW NRTDSPFPAH ECVHHVFENQ VRERPEAIAL VHGDQTLTYC
ELNTRANNLA RQLLDAGVKP GDLVPTLLSR SIDLVTAQLA IVKAGAAYVP IDVKAPADRQ
AYIVSDSGAR LLVTGEHTVV HDSIQAQLFR LGAIDAKNLH QQDASVSIGA IGTSCDTAYV
MYTSGSTGMP KGVMIPHRGI TRLVINNGHA NYGPDDCVVF GANPAFDAST IEVWAPLLNG
GRLVIVDADV YTDAQRLAGL LERYAVTVLF LTPVLLNHYV PIIGQSLSKL RYLLSGGEQG
SLHAYSTLLH LGGRVRLINA YGPTESTTIA TTYEATISNI DALECLPIGR PMANTQVYVL
DKHFQPVPTG AVGELYIGGA GLANGYLNRP DLTAELFLPN VFSKDGGARM YRTGDLVKYL
PDGNLVFMGR NDEQVKIRGF RIELGEIETR LVEHELVTEA VVVALGNEGD KRLVAYVVAE
SAKQLASTLR EHISTSLPEY MVPAAFVRLD ALPFTANGKL DRRHLPAPDA SAFVAQDYEA
PRGDIEISLA EMWTDLLKID QVGRHDNFFT LGGHSLLAVQ MIEQLRRIGL SLSVRALFDT
PVLSVLAASL NTHQAAPETP ANLITAATTV ITPDLLPLID LTQGDIDCIV DQVPGGVANV
QDVYSLSPLQ DGILFHHMMA TEGDPYLLIA GYSFRDRELL DRYLDAVQQI VDRHDILRTA
IVSENLTVPA QVVLRKAPLS ITELKLDPSD GAITSQLMQL YDARKYRIEL RSAPLTRFII
AQDADGRWIM VQLLHHIIGD HSTLEIMDEE IKTILGGKAN TLPAPQPFRN LVAQVRLGLT
VQEHEEFFSK MLSDIDTPAL PYGLSDVHRE GAGVTETHLM LPPNLNDRLR RHAKRLGVSP
ASLCHLAWAQ VIAATSGQRH VVFGTVLFGR MQGGSGADRT MGLFINTLPL RVDIENNTVL
ESVRKVQTDL ATLLEHEHAS LALAQRCSSI PSGSPLFSAL LNYRHNATPF TQVETYDGVE
AIEGHERTNY PFVLSVEDFG TSFGVTVQVV EPYASASVCG YMQQVLQSLA DALEHTPDAP
IQGLKVIPAE EHDLLIHSWN QTESSFPAHQ CVHHVFENQV RERPEAIALV HGDQTLTYRE
LNARVNNLAR QLMDAGVKPG DLVPTLLSRS IDLVIVQLAI VKAGAAYVPI DVKAPADRQA
YIVSDSGARL LVTGEHTVVH NSIQVQLFRL RAIDAKNLHQ QDVSVSIGAI GSSCDTAYVM
YTSGSTGMPK GVMIPHRGIT RLVINNGHAN YGSDDCVVFG ANPAFDASTI EVWAPLLNGG
RLVIVDADVY TDAQRLAGVL ERYAVTVLFL TPVLLNHYVP IIGQSLSKLR YLLSGGEQGS
LHAYSTLLHL GGRVRLINAY GPTESTTIAT TYEATISNID ALECLPIGRP MANTQVYVLD
KHFQPVPTGA VGELYIGGAG LANGYLNRPD LTAELFLPNV FSKDGGARMY RTGDLVKYLP
DGNLVFMGRN DEQVKIRGFR IELGEIEARL VEHELVTEAV VLALGSGSEK RLVAYVVAEH
NEELLHILRE HLAASVPEYM IPAAFVRLDQ LPVTNNGKVD RRALPDPEAT AFASTSYELP
SGDVEIGLAE IWAELLSLDR VGRHDNFFML GGHSLLAVRM AGSVRSRLGL DLKLHSLFAA
PTVAELAQKL VQGGANEDDE YSVIFPLKTS GNRPPLFCIH SGLGLSWPYI GLVKHLHPEQ
PVYGVQARGL DGRTKLATSV EEMTLDYMEQ IRRIQPHGPY HLLGWSFGGT VAHSMATELE
KRGEQVPLLA IMDSTADYSI VAHLKVDEID GGANFEHLVR FGGDVSGEDG WALWERTKPI
NDNSFVLAMQ FKPSVYNGNI LFFRATQKEN DLTPMVNPFS WRPYTNGAIE VHNVECTHIE
MDKPESMAII GRTVTSKLQR S
