ID COBS_PSEDE Reviewed; 332 AA. AC P29933; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 10-AUG-2010, entry version 55. DE RecName: Full=Aerobic cobaltochelatase subunit cobS; DE EC=6.6.1.2; DE AltName: Full=Hydrogenobyrinic acid a,c-diamide cobaltochelatase subunit cobS; GN Name=cobS; OS Pseudomonas denitrificans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=43306; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92011364; PubMed=1917840; RA Cameron B., Guilhot C., Blanche F., Cauchois L., Rouyez M.-C., RA Rigault S., Levy-Schil S., Crouzet J.; RT "Genetic and sequence analyses of a Pseudomonas denitrificans DNA RT fragment containing two cob genes."; RL J. Bacteriol. 173:6058-6065(1991). RN [2] RP CHARACTERIZATION. RX PubMed=1429466; RA Debussche L., Couder M., Thibaut D., Cameron B., Crouzet J., RA Blanche F.; RT "Assay, purification, and characterization of cobaltochelatase, a RT unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic RT acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas RT denitrificans."; RL J. Bacteriol. 174:7445-7451(1992). CC -!- FUNCTION: Catalyzes cobalt insertion in the corrin ring. CC -!- CATALYTIC ACTIVITY: ATP + hydrogenobyrinic acid a,c-diamide + CC Co(2+) + H(2)O = ADP + phosphate + cob(II)yrinic acid a,c-diamide CC + H(2). CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step CC 10/10. CC -!- SUBUNIT: Heterotrimer of cobN, cobS and cobT. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). 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; M62869; AAA25792.1; -; Genomic_DNA. DR ProteinModelPortal; P29933; -. DR BioCyc; MetaCyc:MONOMER-117; -. DR BRENDA; 6.6.1.2; 1952. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0051116; F:cobaltochelatase activity; IEA:EC. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR011704; ATPase_AAA-5. DR InterPro; IPR006537; CobS_ss. DR Pfam; PF07728; AAA_5; 1. DR TIGRFAMs; TIGR01650; PD_CobS; 1. PE 1: Evidence at protein level; KW ATP-binding; Cobalamin biosynthesis; Cytoplasm; Ligase; KW Nucleotide-binding; Porphyrin biosynthesis. FT CHAIN 1 332 Aerobic cobaltochelatase subunit cobS. FT /FTId=PRO_0000089994. SQ SEQUENCE 332 AA; 36983 MW; 8607E19C5C5DA71A CRC64; MMSKIDLDIS NLPDTTISVR EVFGIDTDLR VPAYSKGDAY VPDLDPDYLF DRETTLAILA GFAHNRRVMV SGYHGTGKST HIEQVAARLN WPCVRVNLDS HVSRIDLVGK DAIVVKDGLQ VTEFKDGILP WAYQHNVALV FDEYDAGRPD VMFVIQRVLE SSGRLTLLDQ SRVIRPHPAF RLFATANTVG LGDTTGLYHG TQQINQAQMD RWSIVTTLNY LPHDKEVDIV AAKVKGFTAD KGRETVSKMV RVADLTRAAF INGDLSTVMS PRTVITWAEN AHIFGDIAFA FRVTFLNKCD ELERALVAEH YQRAFGIELK ECAANIVLEA TA //