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Database: UniProt
Entry: K2QZ13_MACPH
LinkDB: K2QZ13_MACPH
Original site: K2QZ13_MACPH 
ID   K2QZ13_MACPH            Unreviewed;       977 AA.
AC   K2QZ13;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:EKG15221.1};
GN   ORFNames=MPH_07555 {ECO:0000313|EMBL:EKG15221.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG15221.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG15221.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG15221.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602402-1};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKG15221.1}.
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DR   EMBL; AHHD01000323; EKG15221.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2QZ13; -.
DR   STRING; 1126212.K2QZ13; -.
DR   VEuPathDB; FungiDB:MPH_07555; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_304208_0_0_1; -.
DR   InParanoid; K2QZ13; -.
DR   OrthoDB; 4950799at2759; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   CDD; cd11063; CYP52; 1.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002974; Cyt_P450_E_CYP52_ascomycetes.
DR   InterPro; IPR047146; Cyt_P450_E_CYP52_fungi.
DR   InterPro; IPR002402; Cyt_P450_E_grp-II.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   PANTHER; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR24287:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01239; EP450IICYP52.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR602402-1};
KW   Iron {ECO:0000256|PIRSR:PIRSR602402-1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602402-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..977
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003866334"
FT   TRANSMEM        677..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         454
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:0000256|PIRSR:PIRSR602402-1"
SQ   SEQUENCE   977 AA;  110128 MW;  CA912A4AA0E2A46B CRC64;
     MVNSGILAAA ALCLLLPLLS RLIKWHRDAQ FARANGCKAA PCDNLLTWTD LLGIGILRKL
     EHHLSQKTLL EFMRKRFEEN GNTFRTRVLL DDFYWTCEPK NIQAMLALKF NDFGVGIDRY
     NNFKPLMGHG IFTSDGAKWE EARALVRPNF VRNQVADLEA FEQHFQNMLT LVPRDGKTPV
     DLKPLFQRMT LDSASEMLFG KSLNSLTVTD SAVASAQFAA AFKKSQTELA RRCRLGRLAD
     WNISKEFLDA CGVTQRFVDD YVEEAVRLRK QSSQGEKKQD EKEPERYIFL HEIAKAIDDP
     IAIRDHLLNV LIPARDSTST LLAAALFAVS KDKRVFAKLR AEVDELGGIY PSFETLKNMR
     YLKWVMNETL RLWPIVPLNG RQANRDVTLP VGGGPDGQSP IHIKAGQNVG FSTYAMHRRK
     DIWGPDADEF IPERWENLRP GWEYLPFNGG PRICIGQQLA LTEGGYTIVR LLQCFKDIES
     LDHSEWREGL ALACSIDQPV TVRMIPWPEH GQSNVHLAVI ASLKRHYGDY VDIHLGSFES
     FRNRVPAGVT FHPIFGRPLT NNFEASDAAD SLSDAVTTTP GFFGAIRGIM KMAYLLHAER
     PEEYIATAES VEGLLEMLQP TLVVVDNFLD AARDAIVKKK RPYALLTPNT LKEVAAGDQG
     FGLFSWPGPA AGYPYPLPWH LVIPNALLFV FFPIWLHFFD QRYALLQRHR HAAGYTGDWP
     IFAGRDPDAP VLCMSHPAAD YAAKIPPGVV CCGPILRDST RVEEVDPELF AWLGRPGRQT
     VLIVLGSLLK VDREYAQNVW DAFRPLLNAR NDVQVLWKLQ KGANYVIEGL ELVGEDRVRV
     VEWLRPDPIA VLRTRKVVCF VNHGGSNSYH EALSTGTPQV ILSPWYDTHD FGNRAEWLGV
     GRWGNKRSAP RCESRELSKC VLDVIGQTPD DEKARRYLCR AQEVAELVTH RAGDSAEGRY
     GRDIAAEIIW NKAQEVL
//
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