FER3_USTMA
ID FER3_USTMA Reviewed; 4830 AA.
AC Q4PEM9; A1A658;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Siderophore peptide synthetase fer3 {ECO:0000303|PubMed:17138696};
DE EC=6.3.2.- {ECO:0000305|PubMed:20070524};
DE AltName: Full=Fe-regulated protein 3 {ECO:0000303|PubMed:17138696};
DE AltName: Full=Ferrichrome A biosynthesis protein fer3 {ECO:0000303|PubMed:20070524};
DE AltName: Full=Nonribosomal peptide synthetase fer3 {ECO:0000303|PubMed:17138696};
DE Short=NRPS fer3 {ECO:0000305};
GN Name=fer3 {ECO:0000303|PubMed:17138696}; ORFNames=UMAG_01434;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION, AND FUNCTION.
RC STRAIN=521 / FGSC 9021;
RX PubMed=17138696; DOI=10.1105/tpc.106.043588;
RA Eichhorn H., Lessing F., Winterberg B., Schirawski J., Kamper J.,
RA Muller P., Kahmann R.;
RT "A ferroxidation/permeation iron uptake system is required for virulence in
RT Ustilago maydis.";
RL Plant Cell 18:3332-3345(2006).
RN [4]
RP FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=20070524; DOI=10.1111/j.1365-2958.2010.07048.x;
RA Winterberg B., Uhlmann S., Linne U., Lessing F., Marahiel M.A.,
RA Eichhorn H., Kahmann R., Schirawski J.;
RT "Elucidation of the complete ferrichrome A biosynthetic pathway in Ustilago
RT maydis.";
RL Mol. Microbiol. 75:1260-1271(2010).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of siderophore ferrichrome A which is
CC contributing to organismal virulence (PubMed:17138696,
CC PubMed:20070524). The first step of ferrichrome A biosynthesis is
CC performed by the HMG-CoA synthase hcs1 which catalyzes the generation
CC of HMG-CoA and CoA using acetoacetyl-CoA and acetyl-CoA as substrates
CC (PubMed:20070524). The enoyl-CoA isomerase/hydratase fer4 then
CC catalyzes the conversion of hcs1-produced HMG-CoA to methylglutaconyl-
CC CoA (PubMed:20070524). The acyltransferase fer5 then fuses the fer4-
CC generated methylglutaconyl-CoA with sid1-generated hydroxyornithine to
CC yield methylglutaconyl hydroxyornithine (PubMed:20070524).
CC Methylglutaconyl hydroxyornithine is then available for use by the NRPS
CC fer3 to generate ferrichrome A (PubMed:20070524).
CC {ECO:0000269|PubMed:17138696, ECO:0000269|PubMed:20070524}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:20070524}.
CC -!- INDUCTION: Expression regulated by iron through the urbs1 transcription
CC factor (PubMed:17138696). {ECO:0000269|PubMed:17138696}.
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. Occasionally,
CC epimerase (E) domains (responsible for l- to d- amino acid conversion)
CC are present within the NRP synthetase. Fer3 has the following
CC architecture: A-T-C-A-T-C-A-T-C-T-C-T-C (PubMed:20070524). The lack of
CC corresponding A domains in the 2 last modules suggests that A domains
CC have to be used iteratively to incorporate the six amino acids in
CC ferrichrome A (PubMed:20070524). {ECO:0000305|PubMed:20070524}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of ferrichrome A but does
CC not affect the production of ferrichrome (PubMed:20070524).
CC {ECO:0000269|PubMed:20070524}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; CM003141; KIS71541.1; -; Genomic_DNA.
DR EMBL; BK004083; DAA04939.1; -; Genomic_DNA.
DR RefSeq; XP_011387303.1; XM_011389001.1.
DR SMR; Q4PEM9; -.
DR STRING; 5270.UM01434P0; -.
DR EnsemblFungi; KIS71541; KIS71541; UMAG_01434.
DR GeneID; 23562458; -.
DR KEGG; uma:UMAG_01434; -.
DR VEuPathDB; FungiDB:UMAG_01434; -.
DR eggNOG; KOG1176; Eukaryota.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000092_1_0_1; -.
DR InParanoid; Q4PEM9; -.
DR OMA; ITMIGEK; -.
DR OrthoDB; 4243at2759; -.
DR BioCyc; MetaCyc:MON-18966; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IBA:GO_Central.
DR GO; GO:0031169; P:ferrichrome biosynthetic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 4.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.559.10; -; 5.
DR Gene3D; 3.40.50.12780; -; 3.
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; 3.
DR Pfam; PF00668; Condensation; 5.
DR Pfam; PF00550; PP-binding; 4.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF47336; SSF47336; 4.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 2: Evidence at transcript level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Virulence.
FT CHAIN 1..4830
FT /note="Siderophore peptide synthetase fer3"
FT /id="PRO_0000441959"
FT DOMAIN 751..833
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1929..2005
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3122..3198
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3685..3760
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4264..4340
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 197..623
FT /note="Adenylation 1"
FT REGION 879..1317
FT /note="Condensation 1"
FT REGION 1358..1781
FT /note="Adenylation 2"
FT REGION 2048..2503
FT /note="Condensation 2"
FT REGION 2573..2977
FT /note="Adenylation 3"
FT REGION 3232..3621
FT /note="Condensation 3"
FT REGION 3779..4199
FT /note="Condensation 4"
FT REGION 4381..4708
FT /note="Condensation 5"
FT MOD_RES 788
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1966
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3159
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3720
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4301
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4830 AA; 528064 MW; B740ACB148A2F13B CRC64;
MAATTLSRLP ALHPYSAVAE PRTLDGTRCF KFMRKSCLEF VKSLVNDEKG EKLISSLAVF
VGHLVGCDAD EALFKVRFGD GQTRITSAGA VHAQVVDVEA SSLPGIAFRF FPPQPTLPKT
LDDDLVVTVN SNSDKDVEFV LEFAQTVPSE AGQGIFAYFC KQVLESTLTE DETPLSILNP
SPVSKLPEHA QLHDSFLDQA EKFPDRMAVQ FLERLDQEDM GQFSKLTYDE LKRLATSLAV
KLQATHAKTS KPQNRQVVVP MLLCPSLELY VSYLAILMAG FAFCPLPVDA PDARLISLLA
QLDTTILLGA NSSQPPQWMP ASVEWINVTD TLAETDQFAK HLTPAKRMQE CAYVLFTSGT
TGTPKGVQIS HYSASISIFS HAACLDPSLL QLSSNTPGST FKWFQFASTV FDPSVMEIFV
TLSSGGTLCS ANRALTLSDL EKVVRLSGAD IMMATPSVAT LLNPERIPKL KFLWTMGECL
NSTVIRRFAA ENGRTTLANA YGPTEASVNC TLLQPFPADF RGSIIGAPLP SCSLAVLHDG
GDSPSGEKRF QAAPRGVTGE LVIGGSHVGI GYLDMPEATA DAFTTFAPLG RVYRTRDRAR
VVWDRDGNPL IEILGRMNAE QVKLSGRRVE LGEIDSILQS SHTIQNAASV IWRPPTSQLQ
SGGGERLVCC IVLAPSAQPQ DAEADCKIIA DAQLPPHMRP WRYIVLPGLP VTVSGKSDRK
QLSKIVAELL SSSAEQGSTK ERSSEQNQVN ANEDPVTQAL IEAICAVCQL DAKSVSMDGD
LFELGMDSLS AMRLLQLLRQ SKVTATAARQ LQVAQILGAK ACRDLIPLLS DTTVSRDAEE
NNVSYPNNTD WSTELRSFED RCRRSALLGL DERTRMRVQK IFPTTATQSG MLTSFLTRPA
SIGSKRSYIN HTVYHFSSVS EACKFFDAFR TVLQKHDIYR TVFVPVDDKL APFAQCVLSP
ASDDDNVSAH TSSTAIDACL KQHLEQIDNA ISLEQPPWHL GLLAPPQEDE VEQSVVVLSL
MHAIFDGGSL DLLQQEVVSL LRDDALQTSL EVRCTELEAT VQHHFTSDLE SSRRFWHQRL
EGVSRTRFPC ANGYKATEQS ALGHASEVTE LYSRSSMDEI VKQARCQRTS ALVLLQTAWN
LVLAAYTEDE SLNYITSGSV HSGRLDEQTQ SCMAPTFNVI PFITRLDQGT GNSATLTSAQ
LLAEATQAST AGLSHLEIPL GALARSGGMP FDTLFAVQRF DAQTCSNATL PWASISYPVM
ANDFAVMVEV WPGSKATEKM RLRLTYSLAV LDAPSAQLLL QQYEDILHSL MREPETTTVQ
QLINGEGLRQ SALSVCRGPL ASENDDSQTE AQLLHSYFEN KAATEPEAIA LEFYFNQDSD
TDGSMEVQRW TYFELNAQAN RLARYLLSVT GKPTLRDLPI PICMERCPEL YVGVLATLKA
GGAWCPIDVQ SPRARQLELI ARTKSRVVLV TPNTSADLGE VQADGQPLTI KVNACDTSQF
HHLSADNLRP TATPATLAYL IWTSGTTGAP KGVMIEHASA VASMQALQQH VKPLQQDMPP
RCLQFSAYTF DVFVQDLFWT WGLGGAIIAA TREIMLGSTA ELIAASQTSH AHLTPAFAAG
LRRDSCPSIT SVTFIGEKLT ESVAADWTSS CASIDKPNDS IAVYNTYGPA EVTVVATLRQ
LFGGEKLQSA NVGVPMQGVT AIVCKNREQP IRPCAKGSIG ELVLAGAQVG RGYLNDKAKT
EAAFTYSPEW KQRLYYTGDY VRMLHDGSIE FIGRRDDLVK LGGIRVELSE ISAALLSVQE
RRKQAAVVER VETMMLSRLD RPTKQVISFL ACPYLAASTD RGVHGAISEP LLLTSGDAIQ
LAHQTLNNVR DVLPPYMVPS MVLVLSRIPQ TASAKIDRAK LQAAYDSADL AQWVSLLSTT
ADDPDNPEGE DGDLQCQVIA AISEITGTST QDINSSSSLV SIGLDSIRAI RLAAKLKQNG
TPLPISTLLA CSTVRMLIRG LATKTGDGHE VAEEDTRNRL LAVKLSEFDK NVREMLPTGS
KQDFEVCIPC STLQEGMLAE TLADPAAYWS DHVLQLDSHI DLARLAEAWR RAAHNIEMLR
TVFAVVSQTA GLEEVQFDKN TDVFALQMVH KSVDITLIDV CDPIRVKSDD RLHQAVSKWT
RSVAQDRADN VFATPLWKVK TFVVQDDSSS GNDQVPLTYA ALCIHHALYD GPSIDIILNR
VRDEYSALSP DMLDDHHNIR LLPTTSLSTQ SEFAYACVAD EQRESILHWE QKLQPRGPAA
MLPDLTSVKD LPSDAKSARF IAASRKLQCT SARPQGVGLS ALIKSAFAIV LAQYVEAEDQ
RHVVLGEILS LRNLHATLST EQGAVGPLLT TQPFSLLLDA ALEQKSAASY LQSNVIVHPS
MQHRFASLAS LAKIMGTRSD QEMFTAMYVY HPRRQPVSVS TKPIWTLLED RSSEIRVEHS
TVLNVFEHDD VEDSLILELS MKEDRISKDM LETLLDQVVS LLTLLLDGAG ETLQALLGKV
GQDQRELASV SHVPRGSRHA GDGSEVDQGH DPLFWLQHYA KNHPSWLAVV IAAGTPETAC
INDAELSSWT YAQLNAKADQ VARLIRSLDL PSEGPIALCM QRSLISIAVT VAIFKCGRTY
LPIDDQLPTE RKRLLISDSR CALVVTEGTC LGELEADCIS SVLNVSKNDF EQSLAALSHR
DDHTELTSIK PRADDGAYLL YTSGSTGKPK GVLVGRANLC SFIDSYAEVV SAECPSTLQL
GGKGRYLGLA GRAFDVHLSQ MFMSWRFGLA LATGERPLLL GDLKATVQTM SITHMSCVPS
LLDQCDLVPQ EVPSLVFLGV GGEKLTDRVR DTLASSLTVL NAYGPTETTI MCTVNRVHPH
SHVRDIGQVL PGNTAVVIDF DDKSRFAPVI RGRAGELCIR GDLVALGYHA LDPSQMATSG
FVTTPDGTRM YRTGDAARMM ADGSLHYLGR RDEQEKIRGQ RLELGEVSRC AIAGADESIQ
ATTLICQHES LAKPLLITLI ATKTSSTGDQ RRDTLPQFLA PSTETGRLAQ HVLQYCKQHL
PSYMVPDLVV GVSHLTQLAA SGKTDVRRLK AWLAAADPTQ LFSFEGRGHA NAQSGSESNV
NRPLSSLERE IASAIRRMLP KCPAEIRPDT SIFDLGIDSL SVIRLAGQLR KEGLAISIGR
LRMHPRVQDI AAELSDSKAL EVDLSVGVKA LESFQARHQD QVQASRVEKV TKVLPCLPSQ
EGMVAISLSS KDEPVYVARI AVRFNDIQPE ATAFAAVSLR RAWRQLSERH SILRTCFDHV
DDVTIAQIVL DAVDIQRHIV TTKTQNSTAA IARAILQDIT VIPPWRIELD DEAGSEPTFV
LHMHHALYDG HSLPLLLNDL ARVIQSIDDD GPESHDQQPG VQEMLESILS VSEQRAERFW
RNTFADFPVN DPSVWTSIAS VQGRAPLRCK ATVQLAPLEA AAKTLQVTLS SLVASALGIA
LCRSLETTAF TVGFVLWGRS LDHVSAESIV APCLTTVPMP FALCADRGSR HVGELIRACH
DWNSSCLAFQ HTSMRQIRRW IGSECRGSLV DLLYSFVQAG ASNSSELART WHLDSVEAET
DAPAAVEVTA DRDRDELRIS AMARHLLPHD GLEGMTENLQ ILLNKIANGT GTNMDLKAAG
IPTSSVASKL ARELPSHSAV SRPLTAAEEQ IRDLAVTMCG VPNTEMLQLD TPFLRIGLDS
IVALRFSARL RREHGLQLSA HDVLAAGTIA GLSKLLDQRQ AEGRSDATVS SSLDSTAARY
KATPLQAGML NGTLASASHD LYVHHHAVLF KQPLDHDRLQ RALQHVVASH DILRTSFHLE
GEPSETKNAV NSLSWYAQVT PFESLRSATE IRVVRSDKTA SAALKEYGTD FIFDGPEKFN
VSPWCAAILH CTSSQDVLVI SMHHSLYDGV SLPSMFADLR ASYHDLTHEL VQRPPFSKAA
DLIASSAHES EQYWLKTLIE FKQPSLLVKK SSRSSTTPSL YRLDERRLSV SLATLKRLSA
ELGATPQAIA MLSWSKVLAV AAGQRDVCFG QVVSGRYLNL PGIEDVSGPL INTVPIRINL
IDDLASNAVT ARDLQERIVA AQPFQHASLG RIQNAWRREH GAHSTFFDTL FVFHNIEGKS
SSASSSKSEL WTALDPSEGP IQTESSTSTV VTTAASEYPV NISVIQDDDG VQIKAGASDA
VGGIDWLPKT LQLFEQVFLD LLERPHRSVG AFPERLAALP LTVGRDGTDK DTSASVGVDA
GRRSLSTAEQ DIVLRHMAKR LNVDAAIINS CPNLFLLGID SLLAICISAD ARSEQVPLTP
FDVLSAGTFA RLTVATETRS EAPRIGVDDS TDTEREMLVG KEAEQEAIEL LKVPSCEVET
VLPLLTGQQQ HIAQWLQRGR RFLEPTFVYA CPSKLDVSKL KSAWNELRRR NAALRTAFVR
LKDRRTLVQV VLAENSLVWR DHERGRLGVV DGSNNLDAAA FEAVQRLNAS PTDLFRPSAR
LTLVQGKQSD LVLVTIHHTS YDAWSMRLMA DELMQLYHNI DQGKLESMRA PVSFADFIDQ
THREALRNRD ATASFWETRL RGASATLVCR GATQSLEQTM HVRKPALQDV DTLEAACRAR
GFGLQVVVIL AYARLLSSEV SDTKITSPTF GFYTAGRASA IDGVGNMIGP TTAMQPMTVA
TAGGDQEDLF ERLRAIQTDL VSRAEHQQDY VDLPVAFDAH LNLLWHKPIT TSMRPPTDDS
NASAPSLLKP YRLPYDSGYF TRHPLMPGNT SVDGDIHEAG AQLYMDVGLD ASTKSLSLGA
RCDRSAMDAQ QLEAFCDRFV GELEKIRAAL
