ID   COBS_SINSX              Reviewed;         332 AA.
AC   P29933;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   11-DEC-2019, entry version 84.
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   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae;
OC   Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=1917840; DOI=10.1128/jb.173.19.6058-6065.1991;
RA   Cameron B., Guilhot C., Blanche F., Cauchois L., Rouyez M.-C., Rigault S.,
RA   Levy-Schil S., Crouzet J.;
RT   "Genetic and sequence analyses of a Pseudomonas denitrificans DNA fragment
RT   containing two cob genes.";
RL   J. Bacteriol. 173:6058-6065(1991).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1429466; DOI=10.1128/jb.174.22.7445-7451.1992;
RA   Debussche L., Couder M., Thibaut D., Cameron B., Crouzet J., Blanche F.;
RT   "Assay, purification, and characterization of cobaltochelatase, a unique
RT   complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-
RT   diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans.";
RL   J. Bacteriol. 174:7445-7451(1992).
CC   -!- FUNCTION: Catalyzes cobalt insertion in the corrin ring.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Co(2+) + H2O + hydrogenobyrinate a,c-diamide = ADP +
CC         cob(II)yrinate a,c diamide + 5 H(+) + phosphate;
CC         Xref=Rhea:RHEA:15341, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48828,
CC         ChEBI:CHEBI:58537, ChEBI:CHEBI:77874, ChEBI:CHEBI:456216; EC=6.6.1.2;
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 {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}.
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DR   EMBL; M62869; AAA25792.1; -; Genomic_DNA.
DR   PRIDE; P29933; -.
DR   KEGG; ag:AAA25792; -.
DR   KO; K09882; -.
DR   BioCyc; MetaCyc:MONOMER-117; -.
DR   UniPathway; UPA00148; UER00221.
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:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR   InterPro; IPR013615; CbbQ_C.
DR   InterPro; IPR025865; CobS_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006537; PD_CobS.
DR   Pfam; PF07728; AAA_5; 1.
DR   Pfam; PF08406; CbbQ_C; 1.
DR   Pfam; PF12556; CobS_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01650; PD_CobS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cobalamin biosynthesis; Cytoplasm; Ligase; Nucleotide-binding;
KW   Porphyrin biosynthesis.
FT   CHAIN           1..332
FT                   /note="Aerobic cobaltochelatase subunit CobS"
FT                   /id="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
//