ID B5GLB3_STRCL Unreviewed; 236 AA. AC B5GLB3; O85726; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAR-2024, entry version 83. DE SubName: Full=Cephalosporin hydroxylase CmcI {ECO:0000313|EMBL:AAC32491.1}; GN Name=cmcI {ECO:0000313|EMBL:AAC32491.1}; GN ORFNames=SCLAV_4208 {ECO:0000313|EMBL:EFG09283.1}; OS Streptomyces clavuligerus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1901 {ECO:0000313|EMBL:AAC32491.1}; RN [1] {ECO:0000313|EMBL:AAC32491.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 3585 {ECO:0000313|EMBL:AAC32491.1}; RX PubMed=9696752; RA Alexander D.C., Jensen S.E.; RT "Investigation of the Streptomyces clavuligerus cephamycin C gene cluster RT and its regulation by the CcaR protein."; RL J. Bacteriol. 180:4068-4079(1998). RN [2] {ECO:0007829|PDB:2BM8, ECO:0007829|PDB:2BM9} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR RP (4FE-4S-S-ADOMET) AND S-ADENOSYL-L-HOMOCYSTEINE. RX PubMed=16527306; DOI=10.1016/J.JMB.2006.02.004; RA Oster L.M., Lester D.R., Terwisscha van Scheltinga A., Svenda M., RA van Lun M., Genereux C., Andersson I.; RT "Insights into cephamycin biosynthesis: the crystal structure of CmcI from RT Streptomyces clavuligerus."; RL J. Mol. Biol. 358:546-558(2006). RN [3] {ECO:0000313|EMBL:EFG09283.1, ECO:0000313|Proteomes:UP000002357} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27064 {ECO:0000313|EMBL:EFG09283.1}, and ATCC 27064 / DSM RC 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602 RC {ECO:0000313|Proteomes:UP000002357}; RX PubMed=20624727; DOI=10.1093/gbe/evq013; RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U., RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L., RA Breitling R., Takano E.; RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich RT evolutionary reservoir of secondary metabolic pathways."; RL Genome Biol. Evol. 2:212-224(2010). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AH006362; AAC32491.1; -; Genomic_DNA. DR EMBL; CM000913; EFG09283.1; -; Genomic_DNA. DR RefSeq; WP_003952496.1; NZ_WMCC01000208.1. DR PDB; 2BM8; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-236. DR PDB; 2BM9; X-ray; 2.94 A; A/B/C/D/E/F=1-236. DR PDB; 2BR3; X-ray; 2.79 A; A/B/C/D/E/F=1-236. DR PDB; 2BR4; X-ray; 2.59 A; A/B/C/D/E/F=1-236. DR PDB; 2BR5; X-ray; 2.83 A; A/B/C/D/E/F=1-236. DR PDBsum; 2BM8; -. DR PDBsum; 2BM9; -. DR PDBsum; 2BR3; -. DR PDBsum; 2BR4; -. DR PDBsum; 2BR5; -. DR STRING; 1901.BB341_07750; -. DR GeneID; 61469711; -. DR KEGG; sclf:BB341_07750; -. DR eggNOG; COG3510; Bacteria. DR OrthoDB; 189417at2; -. DR BioCyc; MetaCyc:MONOMER-13421; -. DR Proteomes; UP000002357; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR007072; RNMT_CmcI. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR Pfam; PF04989; RMNT_CmcI; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2BM8, ECO:0007829|PDB:2BM9}; KW Metal-binding {ECO:0007829|PDB:2BR3, ECO:0007829|PDB:2BR4}; KW Reference proteome {ECO:0000313|Proteomes:UP000002357}; KW S-adenosyl-L-methionine {ECO:0007829|PDB:2BM9, ECO:0007829|PDB:2BR4}. FT BINDING 64 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 64 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BR4" FT BINDING 65 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 65 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BM9, ECO:0007829|PDB:2BR4" FT BINDING 91 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 91 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BM9, ECO:0007829|PDB:2BR4" FT BINDING 95 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 95 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BM9" FT BINDING 116 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 116 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BM9, ECO:0007829|PDB:2BR4" FT BINDING 117 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BM9, ECO:0007829|PDB:2BR4" FT BINDING 121 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 121 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BM9, ECO:0007829|PDB:2BR4" FT BINDING 138 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 138 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BM9, ECO:0007829|PDB:2BR4" FT BINDING 139 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 139 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007829|PDB:2BM9, ECO:0007829|PDB:2BR4" FT BINDING 160 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2BR3" FT BINDING 160 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2BR4" FT BINDING 162 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2BR5" FT BINDING 186 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2BR3" FT BINDING 186 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2BR4" FT BINDING 187 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2BR3" FT BINDING 187 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2BR4" SQ SEQUENCE 236 AA; 27584 MW; FD1EF1B650AF8070 CRC64; MNDYSRQNFL DLNLFRGLGE DPAYHPPVLT DRPRDWPLDR WAEAPRDLGY SDFSPYQWRG LRMLKDPDTQ AVYHDMLWEL RPRTIVELGV YNGGSLAWFR DLTKIMGIDC QVIGIDRDLS RCQIPASDME NITLHQGDCS DLTTFEHLRE MAHPLIFIDD AHANTFNIMK WAVDHLLEEG DYFIIEDMIP YWYRYAPQLL SEYLGAFRDV LSMDMLYANA SSQLDRGVLR RVAAKQ //