MYCCI_MICGR
ID MYCCI_MICGR Reviewed; 388 AA.
AC Q83WF5;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 3.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Mycinamicin VIII C21 methyl hydroxylase {ECO:0000303|PubMed:18804032};
DE EC=1.14.-.- {ECO:0000269|PubMed:18804032};
DE AltName: Full=Cytochrome P450 MycCI {ECO:0000303|PubMed:18804032};
DE AltName: Full=Mycinamicin biosynthesis protein CI {ECO:0000305|PubMed:12583909};
GN Name=mycCI {ECO:0000303|PubMed:12583909};
OS Micromonospora griseorubida.
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=28040;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12583909; DOI=10.1111/j.1574-6968.2003.tb11509.x;
RA Anzai Y., Saito N., Tanaka M., Kinoshita K., Koyama Y., Kato F.;
RT "Organization of the biosynthetic gene cluster for the polyketide macrolide
RT mycinamicin in Micromonospora griseorubida.";
RL FEMS Microbiol. Lett. 218:135-141(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=18804032; DOI=10.1016/j.chembiol.2008.07.014;
RA Anzai Y., Li S., Chaulagain M.R., Kinoshita K., Kato F., Montgomery J.,
RA Sherman D.H.;
RT "Functional analysis of MycCI and MycG, cytochrome P450 enzymes involved in
RT biosynthesis of mycinamicin macrolide antibiotics.";
RL Chem. Biol. 15:950-959(2008).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=A11725;
RX PubMed=22547618; DOI=10.1128/aac.06063-11;
RA Anzai Y., Tsukada S., Sakai A., Masuda R., Harada C., Domeki A., Li S.,
RA Kinoshita K., Sherman D.H., Kato F.;
RT "Function of cytochrome P450 enzymes MycCI and MycG in Micromonospora
RT griseorubida, a producer of the macrolide antibiotic mycinamicin.";
RL Antimicrob. Agents Chemother. 56:3648-3656(2012).
CC -!- FUNCTION: Involved in the biosynthesis of mycinamicin, a 16-membered
CC macrolide antibiotic. Catalyzes hydroxylation at the C21 methyl group
CC of mycinamicin VIII, the earliest macrolide form in the postpolyketide
CC synthase tailoring pathway, leading to mycinamicin VII. Uses ferredoxin
CC MycCII in electron transfer for catalysis.
CC {ECO:0000269|PubMed:18804032, ECO:0000269|PubMed:22547618}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P18326};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34.5 uM for mycinamicin VIII (in the presence of spinach
CC ferredoxin) {ECO:0000269|PubMed:18804032};
CC KM=5.8 uM for mycinamicin VIII (in the presence of MycCII ferredoxin)
CC {ECO:0000269|PubMed:18804032};
CC Note=kcat is 71.7 min(-1) in the presence of spinach ferredoxin. kcat
CC is 104.1 min(-1) in the presence of MycCII ferredoxin.
CC {ECO:0000269|PubMed:18804032};
CC -!- PATHWAY: Antibiotic biosynthesis; mycinamicin biosynthesis.
CC {ECO:0000269|PubMed:22547618, ECO:0000305|PubMed:18804032}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate
CC protomycinolide IV and mycinamicin VIII. {ECO:0000269|PubMed:22547618}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC57023.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB089954; BAC57023.2; ALT_INIT; Genomic_DNA.
DR PDB; 5FOI; X-ray; 2.21 A; A/B=1-388.
DR PDBsum; 5FOI; -.
DR AlphaFoldDB; Q83WF5; -.
DR SMR; Q83WF5; -.
DR KEGG; ag:BAC57023; -.
DR BioCyc; MetaCyc:MON-18365; -.
DR UniPathway; UPA01019; -.
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; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Heme; Iron; Metal-binding;
KW Monooxygenase; NADP; Oxidoreductase.
FT CHAIN 1..388
FT /note="Mycinamicin VIII C21 methyl hydroxylase"
FT /id="PRO_0000434764"
FT BINDING 87
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:P18326"
FT BINDING 91
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:P18326"
FT BINDING 279
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:P18326"
FT BINDING 335
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:P18326"
FT BINDING 337
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:P18326"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 172..192
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:5FOI"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 214..245
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:5FOI"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:5FOI"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:5FOI"
FT HELIX 340..357
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5FOI"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:5FOI"
SQ SEQUENCE 388 AA; 43506 MW; BDEA3761F40C7AFE CRC64;
MVVWPMDRTC AWALPEQYAE FRQRATLVPA KVWDGSPTWL VSRYEHVRAL LVDPRVTVDP
TRQPRLSEAD GDGDGFRSML MLDPPEHTRL RRMFISAFSV RQVETMRPEI EKIVDGILDR
LLALEPPVDI LTHLALPMST QVICHLLGVP YEDREFFQER SELASRPNDD RSMPALIELV
EYLDGLVRTK TAHPDTGLLG TAVTERLLKG EITHQELVNN AVLLLAAGHE TSANQVTLSV
LTLLRHPETA AELREQPELM PNAVDELLRY HSIADGLRRA ATADIVLGDH TIRAGDGLII
LLSSANHDGN TFGAEATFDI HRPARHHVAF GYGPHQCLGQ NLARLEMEVT LGKLFRRVPA
LRLAQEPDAL RVRQGSPIFG IDELLVEW
