CMLI_STRVP
ID CMLI_STRVP Reviewed; 339 AA.
AC F2RB83;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Alpha-N-dichloroacetyl-p-aminophenylserinol N-oxygenase {ECO:0000305};
DE EC=1.14.99.67 {ECO:0000269|PubMed:24347692, ECO:0000269|PubMed:25564306, ECO:0000269|PubMed:27203126, ECO:0000269|PubMed:28823151};
DE AltName: Full=Non-heme di-iron N-oxygenase {ECO:0000303|PubMed:24347692};
GN Name=cmlI {ECO:0000303|PubMed:24347692};
GN OrderedLocusNames=SVEN_0924 {ECO:0000312|EMBL:CCA54211.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=953739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Chandra G., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=24347692; DOI=10.1016/j.tet.2012.06.036;
RA Lu H., Chanco E., Zhao H.;
RT "CmlI is an N-oxygenase in the biosynthesis of chloramphenicol.";
RL Tetrahedron 68:7651-7654(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX PubMed=25564306; DOI=10.1021/ja511649n;
RA Makris T.M., Vu V.V., Meier K.K., Komor A.J., Rivard B.S., Muenck E.,
RA Que L. Jr., Lipscomb J.D.;
RT "An unusual peroxo intermediate of the arylamine oxygenase of the
RT chloramphenicol biosynthetic pathway.";
RL J. Am. Chem. Soc. 137:1608-1617(2015).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, AND COFACTOR.
RX PubMed=27203126; DOI=10.1021/jacs.6b03341;
RA Komor A.J., Rivard B.S., Fan R., Guo Y., Que L. Jr., Lipscomb J.D.;
RT "Mechanism for six-electron aryl-N-oxygenation by the non-heme diiron
RT enzyme CmlI.";
RL J. Am. Chem. Soc. 138:7411-7421(2016).
RN [5]
RP CATALYTIC ACTIVITY, REACTION MECHANISM, AND COFACTOR.
RX PubMed=28823151; DOI=10.1021/acs.biochem.7b00695;
RA Komor A.J., Rivard B.S., Fan R., Guo Y., Que L. Jr., Lipscomb J.D.;
RT "CmlI N-oxygenase catalyzes the final three steps in chloramphenicol
RT biosynthesis without dissociation of intermediates.";
RL Biochemistry 56:4940-4950(2017).
RN [6] {ECO:0007744|PDB:5HYG, ECO:0007744|PDB:5HYH}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 33-339 IN COMPLEX WITH IRON, AND
RP COFACTOR.
RX PubMed=27229511; DOI=10.1007/s00775-016-1363-x;
RA Knoot C.J., Kovaleva E.G., Lipscomb J.D.;
RT "Crystal structure of CmlI, the arylamine oxygenase from the
RT chloramphenicol biosynthetic pathway.";
RL J. Biol. Inorg. Chem. 21:589-603(2016).
CC -!- FUNCTION: Involved in chloramphenicol biosynthesis (PubMed:24347692,
CC PubMed:25564306). Catalyzes the six-electron oxidation of an aryl-amine
CC precursor of chloramphenicol (NH2-CAM) to yield the aryl-nitro group of
CC chloramphenicol (CAM) (PubMed:24347692, PubMed:25564306,
CC PubMed:27203126). During catalysis, upon exposure of the diferrous
CC cluster to O(2), ClmI forms an exceptionally long-lived peroxo
CC intermediate (CmlI-peroxo), which reacts with NH2-CAM to form CAM
CC (PubMed:25564306, PubMed:27203126). {ECO:0000269|PubMed:24347692,
CC ECO:0000269|PubMed:25564306, ECO:0000269|PubMed:27203126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + alpha-N-dichloroacetyl-p-aminophenylserinol + 2 O2 = A +
CC chloramphenicol + 2 H2O; Xref=Rhea:RHEA:58884, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:17698, ChEBI:CHEBI:47325; EC=1.14.99.67;
CC Evidence={ECO:0000269|PubMed:24347692, ECO:0000269|PubMed:25564306,
CC ECO:0000269|PubMed:27203126, ECO:0000269|PubMed:28823151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58885;
CC Evidence={ECO:0000269|PubMed:24347692, ECO:0000269|PubMed:25564306,
CC ECO:0000269|PubMed:27203126, ECO:0000269|PubMed:28823151};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:25564306, ECO:0000269|PubMed:27203126,
CC ECO:0000269|PubMed:27229511, ECO:0000269|PubMed:28823151};
CC Note=Contains a nonheme dinuclear iron cluster that stabilizes a peroxo
CC intermediate. {ECO:0000269|PubMed:25564306,
CC ECO:0000269|PubMed:27203126, ECO:0000269|PubMed:27229511,
CC ECO:0000269|PubMed:28823151};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:24347692,
CC ECO:0000269|PubMed:25564306}.
CC -!- SIMILARITY: Belongs to the AurF N-oxygenase family. {ECO:0000305}.
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DR EMBL; FR845719; CCA54211.1; -; Genomic_DNA.
DR RefSeq; WP_015032130.1; NZ_CP029197.1.
DR PDB; 5HYG; X-ray; 2.03 A; A=33-339.
DR PDB; 5HYH; X-ray; 2.03 A; A=33-339.
DR PDBsum; 5HYG; -.
DR PDBsum; 5HYH; -.
DR AlphaFoldDB; F2RB83; -.
DR SMR; F2RB83; -.
DR STRING; 953739.SVEN_0924; -.
DR EnsemblBacteria; CCA54211; CCA54211; SVEN_0924.
DR KEGG; sve:SVEN_0924; -.
DR PATRIC; fig|953739.5.peg.2970; -.
DR eggNOG; ENOG502ZAK9; Bacteria.
DR HOGENOM; CLU_070306_0_0_11; -.
DR OMA; HTLMHIN; -.
DR BioCyc; MetaCyc:MON-20699; -.
DR BRENDA; 1.14.99.67; 6106.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR025859; AurF.
DR InterPro; IPR012348; RNR-like.
DR Pfam; PF11583; AurF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..339
FT /note="Alpha-N-dichloroacetyl-p-aminophenylserinol N-
FT oxygenase"
FT /id="PRO_0000447294"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27229511"
FT BINDING 144
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27229511"
FT BINDING 144
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27229511"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27229511"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27229511"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27229511"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27229511"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27229511"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27229511"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 87..111
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 131..162
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 190..216
FT /evidence="ECO:0007829|PDB:5HYG"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 223..253
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 256..274
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:5HYG"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:5HYG"
SQ SEQUENCE 339 AA; 38249 MW; BEBB026FE7AB8BD3 CRC64;
MRDHTDEKSE AAGNDDGHVR IGGLPAFDPD DPAENAVINR LVGNWHRRAA VKREEPDVYA
LFDPGRPDFR EDMIPFRGHP IWERLSDETR SRLLSWGWVA YNRNTVLIEQ RIANPAFELV
IGGAYPGLGG QQLELAVAQA MVDEQYHTLM HINGSAVTRR MRRSDFSDRV LPDSHITTIH
QEHLDRCEEP WQRSLTTLGF ATVAEISINA YLDLLADDQE IQVVNSTTVK LHNRDEYCHA
SISGEMMKQV YEALPADRRR FLLEKVVAGL EAFVAPDFTT WESIVAFEGV PGWEKAAAEV
REAQGGTHLV QDHSGIHTLL TEMDVLDQVE FGWGTTVTR
