ID COBH_SINSX Reviewed; 210 AA. AC P21638; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 13-SEP-2023, entry version 109. DE RecName: Full=Precorrin-8X methylmutase; DE EC=5.4.99.61; DE AltName: Full=HBA synthase; DE AltName: Full=Precorrin isomerase; GN Name=cobH; OS Sinorhizobium sp. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=42445; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=SC510; RX PubMed=2211521; DOI=10.1128/jb.172.10.5980-5990.1990; RA Crouzet J., Cameron B., Cauchois L., Rigault S., Rouyez M.-C., Blanche F., RA Thibaut D., Debussche L.; RT "Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans RT fragment carrying eight genes involved in transformation of precorrin-2 to RT cobyrinic acid."; RL J. Bacteriol. 172:5980-5990(1990). RN [2] RP PROTEIN SEQUENCE OF 2-18, FUNCTION, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=1732194; DOI=10.1128/jb.174.3.1043-1049.1992; RA Thibaut D., Couder M., Famechon A., Debussche L., Cameron B., Crouzet J., RA Blanche F.; RT "The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed RT by the cobH gene product with precorrin-8x as the substrate."; RL J. Bacteriol. 174:1043-1049(1992). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-210 OF APOENZYME AND IN COMPLEX RP WITH HYDROGENOBYRINATE, SUBUNIT, ACTIVE SITE, AND REACTION MECHANISM. RX PubMed=11470433; DOI=10.1016/s0969-2126(01)00618-9; RA Shipman L.W., Li D., Roessner C.A., Scott A.I., Sacchettini J.C.; RT "Crystal structure of precorrin-8x methyl mutase."; RL Structure 9:587-596(2001). CC -!- FUNCTION: Catalyzes the conversion of precorrin-8X to CC hydrogenobyrinate. {ECO:0000269|PubMed:1732194}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3 H(+) + precorrin-8X = hydrogenobyrinate; CC Xref=Rhea:RHEA:22512, ChEBI:CHEBI:15378, ChEBI:CHEBI:58581, CC ChEBI:CHEBI:77873; EC=5.4.99.61; CC Evidence={ECO:0000269|PubMed:1732194}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.91 uM for precorrin-8X {ECO:0000269|PubMed:1732194}; CC Vmax=230 nmol/h/mg enzyme {ECO:0000269|PubMed:1732194}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 8/10. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11470433}. CC -!- SIMILARITY: Belongs to the CobH/CbiC family. {ECO:0000305}. CC -!- CAUTION: Was originally thought to originate from Pseudomonas CC denitrificans, but similarity searches show that the sequence is much CC closer to Sinorhizobium. The entry's taxonomy has been changed. CC {ECO:0000305}. 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; M59301; AAA25796.1; -; Genomic_DNA. DR PDB; 1F2V; X-ray; 2.10 A; A=2-210. DR PDB; 1I1H; X-ray; 2.60 A; A=2-210. DR PDBsum; 1F2V; -. DR PDBsum; 1I1H; -. DR AlphaFoldDB; P21638; -. DR SMR; P21638; -. DR DrugBank; DB02460; Hydrogenobyrinic acid. DR KEGG; ag:AAA25796; -. DR BioCyc; MetaCyc:MONOMER-115; -. DR SABIO-RK; P21638; -. DR UniPathway; UPA00148; UER00219. DR EvolutionaryTrace; P21638; -. DR GO; GO:0016993; F:precorrin-8X methylmutase activity; IEA:UniProtKB-EC. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.10230; Cobalamin biosynthesis CobH/CbiC, precorrin-8X methylmutase; 1. DR InterPro; IPR003722; Cbl_synth_CobH/CbiC. DR InterPro; IPR036588; CobH/CbiC_sf. DR PANTHER; PTHR43588; COBALT-PRECORRIN-8 METHYLMUTASE; 1. DR PANTHER; PTHR43588:SF1; COBALT-PRECORRIN-8 METHYLMUTASE; 1. DR Pfam; PF02570; CbiC; 1. DR SUPFAM; SSF63965; Precorrin-8X methylmutase CbiC/CobH; 1. PE 1: Evidence at protein level; KW 3D-structure; Cobalamin biosynthesis; Direct protein sequencing; Isomerase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1732194" FT CHAIN 2..210 FT /note="Precorrin-8X methylmutase" FT /id="PRO_0000135926" FT ACT_SITE 43 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000305|PubMed:11470433" FT BINDING 17 FT /ligand="substrate" FT BINDING 40 FT /ligand="substrate" FT HELIX 10..24 FT /evidence="ECO:0007829|PDB:1F2V" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:1I1H" FT HELIX 32..45 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 48..53 FT /evidence="ECO:0007829|PDB:1F2V" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 60..69 FT /evidence="ECO:0007829|PDB:1F2V" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 79..84 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:1F2V" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 104..112 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 120..124 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 125..128 FT /evidence="ECO:0007829|PDB:1F2V" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 139..150 FT /evidence="ECO:0007829|PDB:1F2V" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:1F2V" FT STRAND 165..168 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 169..178 FT /evidence="ECO:0007829|PDB:1F2V" FT STRAND 185..188 FT /evidence="ECO:0007829|PDB:1F2V" FT HELIX 195..206 FT /evidence="ECO:0007829|PDB:1F2V" SQ SEQUENCE 210 AA; 22064 MW; 506D1C4C5D972B3F CRC64; MPEYDYIRDG NAIYERSFAI IRAEADLSRF SEEEADLAVR MVHACGSVEA TRQFVFSPDF VSSARAALKA GAPILCDAEM VAHGVTRARL PAGNEVICTL RDPRTPALAA EIGNTRSAAA LKLWSERLAG SVVAIGNAPT ALFFLLEMLR DGAPKPAAIL GMPVGFVGAA ESKDALAENS YGVPFAIVRG RLGGSAMTAA ALNSLARPGL //