ID   COBT_SINSX              Reviewed;         631 AA.
AC   P29934;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Aerobic cobaltochelatase subunit CobT;
DE            EC=6.6.1.2;
DE   AltName: Full=Hydrogenobyrinic acid a,c-diamide cobaltochelatase subunit CobT;
GN   Name=cobT;
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=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; AAA25793.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29934; -.
DR   KEGG; ag:AAA25793; -.
DR   BioCyc; MetaCyc:MON-118; -.
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   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR006538; CobT.
DR   InterPro; IPR025861; CobT_VWA_dom.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF06213; CobT; 1.
DR   Pfam; PF11775; CobT_C; 1.
DR   PIRSF; PIRSF031715; Cob_chel_CobT; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   TIGRFAMs; TIGR01651; CobT; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cobalamin biosynthesis; Cytoplasm; Ligase; Nucleotide-binding;
KW   Porphyrin biosynthesis.
FT   CHAIN           1..631
FT                   /note="Aerobic cobaltochelatase subunit CobT"
FT                   /id="PRO_0000089995"
FT   DOMAIN          412..631
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          218..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..239
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..292
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  70367 MW;  97BF7CD242370E6F CRC64;
     MSSNSKAKPT TRENAAEPFK RALSGCIRSI AGDAEVEVAF ANERPGMTGE RIRLPELSKR
     PTLQELAVTR GLGDSMALRK ACTHARIQRT MSPQGADARA IFDAVEQARV EAIGSLRMAG
     VAKNLNVMLE EKYAKANFAT IERQADAPLG EAVALLVREK LTGQKPPASA GKVLDLWREF
     IEGKAAGDIE HLSSTINNQQ AFARVVRDML TSMEVAEKYG DDDNEPDEQE SETDEDQPRS
     QEQDENASDE EAGDDAAPAD ENQAAEEQME EGEMDGAEIS DDDLQDEGDE DSETPGEVKR
     PNQPFADFNE KVDYAVFTRE FDETIASEEL CDEAELDRLR AFLDKQLAHL QGAVGRLANR
     LQRRLMAQQN RSWEFDLEEG YLDSARLQRI IIDPMQPLSF KREKDTNFRD TVVTLLIDNS
     GSMRGRPITV AATCADILAR TLERCGVKVE ILGFTTKAWK GGQSREKWLA GGKPQAPGRL
     NDLRHIVYKS ADAPWRRARR NLGLMMREGL LKENIDGEAL IWAHERLMAR REQRRILMMI
     SDGAPVDDST LSVNPGNYLE RHLRAVIEQI ETRSPVELLA IGIGHDVTRY YRRAVTIVDA
     DELAGAMTEQ LAALFEDESQ RRGSSRLRRA G