ID   COBN_SINSX              Reviewed;        1275 AA.
AC   P29929;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Aerobic cobaltochelatase subunit CobN;
DE            EC=6.6.1.2;
DE   AltName: Full=Hydrogenobyrinic acid a,c-diamide cobaltochelatase subunit CobN;
GN   Name=cobN;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=1655697; DOI=10.1128/jb.173.19.6074-6087.1991;
RA   Crouzet J., Levy-Schil S., Cameron B., Cauchois L., Rigault S.,
RA   Rouyez M.-C., Blanche F., Debussche L., Thibaut D.;
RT   "Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair
RT   Pseudomonas denitrificans DNA fragment containing five cob genes and
RT   identification of structural genes encoding Cob(I)alamin
RT   adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide
RT   kinase-cobinamide phosphate guanylyltransferase.";
RL   J. Bacteriol. 173:6074-6087(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   -!- SIMILARITY: Belongs to the CobN 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}.
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DR   EMBL; M62866; AAA25780.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29929; -.
DR   SMR; P29929; -.
DR   KEGG; ag:AAA25780; -.
DR   BioCyc; MetaCyc:MON-121; -.
DR   BRENDA; 6.6.1.2; 5114.
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: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   CDD; cd10150; CobN_like; 1.
DR   InterPro; IPR011953; Cobalto_CobN.
DR   InterPro; IPR003672; CobN/Mg_chltase.
DR   PANTHER; PTHR44119; PTHR44119; 1.
DR   Pfam; PF02514; CobN-Mg_chel; 1.
DR   TIGRFAMs; TIGR02257; cobalto_cobN; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cobalamin biosynthesis; Cytoplasm; Ligase; Nucleotide-binding;
KW   Porphyrin biosynthesis.
FT   CHAIN           1..1275
FT                   /note="Aerobic cobaltochelatase subunit CobN"
FT                   /id="PRO_0000089991"
SQ   SEQUENCE   1275 AA;  138056 MW;  3FDF2858434E4C78 CRC64;
     MHLLLAQKGT IADGNEAIDL GQTPADILFL SAADTELSSI AAAHGRRDGG LSLRIASLMS
     LMHPMSVDTY VERTARHAKL IVVRPLGGAS YFRYLLEALH AAAVTHRFEI AVLPGDDKPD
     PGLEPFSTVA ADDRQRLWAY FTEGGSDNAG LFLDYAAALV TGAEKPQPAK PLLKAGIWWP
     GAGVIGVSEW QSLVQGRMVA REGFEPPTVG ICFYRALVQS GETRPVEALI DALEAEGVRA
     LPVFVSSLKD AVSVGTLQAI FSEAAPDVVM NATGFAVSSP GADRQPTVLE STGAPVLQVI
     FSGSSRAQWE TSPQGLMARD LAMNVALPEV DGRILARAVS FKAASIYDAK VEANIVGHEP
     LEGRVRFAAD LAVNWANVRR AEPAERRIAI VMANYPNRDG RLGNGVGLDT PAGTVEVLSA
     MAREGYAVGE VPADGDALIR FLMAGPTNAA SHDREIRERI SLNDYKTFFD SLPKQIKDEV
     AGRWGVPEAD PFFLDGAFAL PLARFGEVIV GIQPARGYNI DPKESYHSPD LVPPHGYLAF
     YAFLRQQFGA QAIVHMGKHG NLEWLPGKAL ALSETCYPEA IFGPLPHIYP FIVNDPGEGT
     QAKRRTSAVI IDHLTPPLTR AESYGPLKDL EALVDEYYDA AGGDPRRLRL LSRQILDLVR
     DIGLDSDAGI DRGDSDDKAL EKLDAYLCDL KEMQIRDGLH IFGVAPEGRL LTDLTVALAR
     VPRGLGEGGD QSLQRAIAAD AGLRGFAIPT SAGGNPARDA QPFDPLDCVM SDTWTGPKPS
     ILADLSDAPW RTAGDTVERI ELLAANLVSG ELACPDHWAN TRAVLGEIET RLKPSISNSG
     AAEMTGFLTG LSGRFVAPGP SGAPTRGRPD VLPTGRNFYS VDSRAVPTPA AYELGKKSAE
     LLIRRYLQDH GEWPSSFGLT AWGTANMRTG GDDIAQALAL IGAKPTWDMV SRRVMGYEIV
     PLAVLGRPRV DVTLRISGFF RDAFPDQIAL FDKAIRAVAL EEDDADNMIA ARMRAESRRL
     EAEGVEAAEA ARRASYRVFG AKPGAYGAAL QALIDEKGWE TKADLAEAYL TWGAYAYGAG
     EEGKAERDLF EERLRTIEAV VQNQDNREHD LLDSDDYYQF EGGMSAAAEQ LGGHRPAIYH
     NDHSRPEKPV IRSLEEEIGR VVRARVVNPK WIDGVMRHGY KGAFEIAATV DYMFAFAATT
     GAVRDHHFEA AYQAFIVDER VADFMRDKNP AAFAELAERL LEAIDRNLWT PRSNSARFEL
     AGIGTAATRL RAGNE