PUL2_KLULA
ID PUL2_KLULA Reviewed; 511 AA.
AC Q6CSN2;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cytochrome P450 monooxygenase PUL2 {ECO:0000303|PubMed:30297402};
DE EC=1.-.-.- {ECO:0000305|PubMed:30297402};
DE AltName: Full=Pulcherrimin biosynthesis cluster protein 2 {ECO:0000303|PubMed:30297402};
GN Name=PUL2 {ECO:0000303|PubMed:30297402}; OrderedLocusNames=KLLA0_C19206g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
RX PubMed=30297402; DOI=10.1073/pnas.1806268115;
RA Krause D.J., Kominek J., Opulente D.A., Shen X.X., Zhou X., Langdon Q.K.,
RA DeVirgilio J., Hulfachor A.B., Kurtzman C.P., Rokas A., Hittinger C.T.;
RT "Functional and evolutionary characterization of a secondary metabolite
RT gene cluster in budding yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:11030-11035(2018).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the PUL gene cluster
CC that mediates the formation of pulcherrimin, a red iron-containing
CC pigment composed of two cyclized and modified leucine molecules that
CC acts as a siderophore, a chelator that binds iron outside the cell for
CC subsequent uptake (PubMed:30297402). Two leucine molecules are cyclized
CC via a cyclodipeptide synthase, and the resulting diketopiperazine is
CC oxidized by a cytochrome P450 monooxygenase to generate pulcherriminic
CC acid (PA), which can then spontaneously bind iron to form pulcherrimin
CC (PubMed:30297402). The probable cyclodipeptide synthase PUL1 and the
CC cytochrome P450 monooxygenase PUL2 encode the enzymes responsible for
CC the two-step pulcherrimin biosynthesis pathway (Probable).
CC {ECO:0000269|PubMed:30297402, ECO:0000305|PubMed:30297402}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:30297402}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impairs pulcherrimin production and subsequent
CC red pigmentation. {ECO:0000269|PubMed:30297402}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CR382123; CAH01908.1; -; Genomic_DNA.
DR RefSeq; XP_453057.1; XM_453057.1.
DR AlphaFoldDB; Q6CSN2; -.
DR SMR; Q6CSN2; -.
DR STRING; 28985.XP_453057.1; -.
DR EnsemblFungi; CAH01908; CAH01908; KLLA0_C19206g.
DR GeneID; 2892619; -.
DR KEGG; kla:KLLA0_C19206g; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_042557_0_0_1; -.
DR InParanoid; Q6CSN2; -.
DR OMA; AFLRFGF; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..511
FT /note="Cytochrome P450 monooxygenase PUL2"
FT /id="PRO_0000445897"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 462
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 511 AA; 59318 MW; C207C71D412C3798 CRC64;
MLADILIPLI KKNWMAFVYF TPVLFVVLYL LKEWRAAYGF NNLGQTVAAP FGYERKTLPY
NKENCARTKF LDGKSLSIKN RDQCGDLYLQ RSGTYKEIVL TTPKQLMEYY KSNSKNHSKL
DSFGAGAFLV ALLGECLGFQ NGSEWLSMRK VFDSFFTHKA AVENFPVMID YISEWIKDLD
TEQISDIDPL QLVSDLPFTC IAKYLYGSEL CSKQFLQALK DLIPMHTELM HYSFLTVAGR
FKIFQYFPSK KMKQVSQFQR QFIDLSLKQV ELSRQSGQET VVEKLYRHVE SGKFTFNNWI
QTIDEILFAN IEVTSTVMAW ALVEMGSNIE EQNRLRCEIL KVKEQSSKDD FNKETDPMQR
YMKLTDTYLQ YCVWETLRMH PLLWFSFPEI SSETLFIDGI RISPNTPIVV DQYQINYNSP
IWNPSDKPKD FGKKFAPSRF ENITLRDALY SQVTFGAGSR KCLGRNFAEL LIKSELAYIL
SKYKVTLTEK VEFSKDTFVV QPKTKIQLTA L
