FER5_USTMA
ID FER5_USTMA Reviewed; 427 AA.
AC Q4PEN1; A1A656;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Acyltransferase fer5 {ECO:0000303|PubMed:17138696};
DE EC=2.3.-.- {ECO:0000269|PubMed:20070524};
DE AltName: Full=Fe-regulated protein 5 {ECO:0000303|PubMed:17138696};
DE AltName: Full=Ferrichrome A biosynthesis protein fer5 {ECO:0000303|PubMed:20070524};
GN Name=fer5 {ECO:0000303|PubMed:17138696}; ORFNames=UMAG_01432;
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, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
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: Acyltransferase; part of the gene cluster that mediates the
CC biosynthesis of siderophore ferrichrome A which is contributing to
CC organismal virulence (PubMed:17138696, PubMed:20070524). The first step
CC of ferrichrome A biosynthesis is performed by the HMG-CoA synthase hcs1
CC which catalyzes the generation of HMG-CoA and CoA using acetoacetyl-CoA
CC and acetyl-CoA as substrates (PubMed:20070524). The enoyl-CoA
CC isomerase/hydratase fer4 then catalyzes the conversion of hcs1-produced
CC HMG-CoA to methylglutaconyl-CoA (PubMed:20070524). The acyltransferase
CC fer5 then fuses the fer4-generated methylglutaconyl-CoA with sid1-
CC generated hydroxyornithine to yield methylglutaconyl hydroxyornithine
CC (PubMed:20070524). Methylglutaconyl hydroxyornithine is then available
CC for use by the NRPS 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 -!- 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 lysine N-acyltransferase mbtK family.
CC {ECO:0000305}.
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DR EMBL; CM003141; KIS71539.1; -; Genomic_DNA.
DR EMBL; BK004083; DAA04937.1; -; Genomic_DNA.
DR RefSeq; XP_011387301.1; XM_011388999.1.
DR AlphaFoldDB; Q4PEN1; -.
DR SMR; Q4PEN1; -.
DR STRING; 5270.UM01432P0; -.
DR EnsemblFungi; KIS71539; KIS71539; UMAG_01432.
DR GeneID; 23562456; -.
DR KEGG; uma:UMAG_01432; -.
DR VEuPathDB; FungiDB:UMAG_01432; -.
DR eggNOG; ENOG502RZMI; Eukaryota.
DR HOGENOM; CLU_039848_7_0_1; -.
DR InParanoid; Q4PEN1; -.
DR OMA; CNITVGE; -.
DR OrthoDB; 985920at2759; -.
DR BioCyc; MetaCyc:MON-18965; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR019432; Acyltransferase_MbtK/IucB-like.
DR SMART; SM01006; AlcB; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase; Virulence.
FT CHAIN 1..427
FT /note="Acyltransferase fer5"
FT /id="PRO_0000441961"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 427 AA; 48098 MW; 534F66E7750F1D07 CRC64;
MTAATSVQPS PAPRQPGLRA TFNPRKEEKV FLARGAHAFT LPGRRASVNV EVDVEAESDE
AALDAKETTI TVSYAEKGQE SSWSAAKWIK LDRLAKTSQH GVVNEDRATY QQAWSLELLD
EAVEPARAIW SALYAFWIRH KRSDRLAVLL KGTQATKVRS YVFEAGLGFK SPCETDLILL
DRNAFWQGAG APAGLHWLQT PVPTRGLFPY VLDFTQSTSP PVLATHPLRP PKPAPGSVVY
SRYVFSCSQH LELVHIDVSN PQHFDAYTRW QNSDRVNHGW REKGSDEKHR KYITEKNDDP
HAMGVLVLWD GVPAGYGEMV WSKEDGMAAF VGGLGNYDQG THLLIGEEQF RGKHRFTACM
VSLKHACFLR DPRTEVVVGE PRYDLDIIPL LATFLPQEIR KEVELPHKRA VFFVLRRDRF
LEEGILE
