FER4_USTMA
ID FER4_USTMA Reviewed; 274 AA.
AC Q4PEN0; A1A657;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Enoyl-CoA isomerase/hydratase fer4 {ECO:0000303|PubMed:17138696};
DE EC=4.2.1.17 {ECO:0000269|PubMed:20070524};
DE AltName: Full=Fe-regulated protein 4 {ECO:0000303|PubMed:17138696};
DE AltName: Full=Ferrichrome A biosynthesis protein fer4 {ECO:0000303|PubMed:20070524};
GN Name=fer4 {ECO:0000303|PubMed:17138696}; ORFNames=UMAG_01433;
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: Enoyl-CoA isomerase/hydratase; part of the gene cluster that
CC 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17;
CC Evidence={ECO:0000305|PubMed:17138696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC ChEBI:CHEBI:137480; EC=4.2.1.17;
CC Evidence={ECO:0000305|PubMed:17138696};
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 enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; CM003141; KIS71540.1; -; Genomic_DNA.
DR EMBL; BK004083; DAA04938.1; -; Genomic_DNA.
DR RefSeq; XP_011387302.1; XM_011389000.1.
DR AlphaFoldDB; Q4PEN0; -.
DR SMR; Q4PEN0; -.
DR STRING; 5270.UM01433P0; -.
DR EnsemblFungi; KIS71540; KIS71540; UMAG_01433.
DR GeneID; 23562457; -.
DR KEGG; uma:UMAG_01433; -.
DR VEuPathDB; FungiDB:UMAG_01433; -.
DR eggNOG; KOG1679; Eukaryota.
DR HOGENOM; CLU_009834_7_6_1; -.
DR InParanoid; Q4PEN0; -.
DR OMA; ESARFCT; -.
DR OrthoDB; 1123666at2759; -.
DR BioCyc; MetaCyc:MON-18964; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isomerase; Lyase; Reference proteome; Virulence.
FT CHAIN 1..274
FT /note="Enoyl-CoA isomerase/hydratase fer4"
FT /id="PRO_0000441960"
FT COILED 79..109
FT /evidence="ECO:0000255"
FT BINDING 77..81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 148
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
SQ SEQUENCE 274 AA; 29825 MW; 6BA3CF119D99F6D0 CRC64;
MTASALAYLE PDSSAELTGV YHLVLDRPEA RNAISRSLLQ DVLQCLQVLV CKITQPKQDE
PLPRVLILRA NGPCFCAGAD LKERREMSEA EVIEFLQDLR HMLEQVEKLP IPTLAAIDGP
ALGGGLELAL ACDFRIAAET VSKIGFPEVK LGIIPGAGGT QRAPRIIGMQ RAKELIYTGT
QLNATQAKDL GLIDHVAPGS TCLKLCQELA QQMMPSAPLA LRAAKMAISM GANVELARGL
DLEWACYEPL LESKDRREAL DAFQQKRKPI FTGK
