AC MF_00027; DC Protein; auto TR HAMAP; MF_00027; -; 1; level=0 XX Names: CobB/CbiA XX case or or or ID COBB DE RecName: Full=Hydrogenobyrinate a,c-diamide synthase; DE EC=6.3.5.9; DE AltName: Full=Hydrogenobyrinic acid a,c-diamide synthase; GN Name=cobB; else case or or or ID CBIA DE RecName: Full=Cobyrinate a,c-diamide synthase; DE EC=6.3.5.11; DE AltName: Full=Cobyrinic acid a,c-diamide synthetase; DE AltName: Full=Ni-sirohydrochlorin a,c-diamide synthase; DE EC=6.3.5.12; DE AltName: Full=Ni-sirohydrochlorin a,c-diamide synthetase; GN Name=cbiA; Synonyms=cfbB; else ID CBIA DE RecName: Full=Cobyrinate a,c-diamide synthase; DE EC=6.3.5.11; DE AltName: Full=Cobyrinic acid a,c-diamide synthetase; GN Name=cbiA; end case XX case or or or CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate CC groups at positions a and c of hydrogenobyrinate, using either L- CC glutamine or ammonia as the nitrogen source. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ATP + 2 H2O + hydrogenobyrinate + 2 L-glutamine = 2 ADP + 2 CC H(+) + hydrogenobyrinate a,c-diamide + 2 L-glutamate + 2 phosphate; CC Xref=Rhea:RHEA:12544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:77873, ChEBI:CHEBI:77874, CC ChEBI:CHEBI:456216; EC=6.3.5.9; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 9/10. CC -!- DOMAIN: Comprises of two domains. The C-terminal domain contains the CC binding site for glutamine and catalyzes the hydrolysis of this CC substrate to glutamate and ammonia. The N-terminal domain is CC anticipated to bind ATP and hydrogenobyrinate and catalyzes the CC ultimate synthesis of the diamide product. The ammonia produced via the CC glutaminase domain is probably translocated to the adjacent domain via CC a molecular tunnel, where it reacts with an activated intermediate. CC -!- MISCELLANEOUS: The a and c carboxylates of hydrogenobyrinate are CC activated for nucleophilic attack via formation of a phosphorylated CC intermediate by ATP. CobB catalyzes first the amidation of the c- CC carboxylate, and then that of the a-carboxylate. else case or or or CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate CC groups at positions a and c of cobyrinate, using either L-glutamine or CC ammonia as the nitrogen source. Involved in the biosynthesis of the CC unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic CC group of methyl-coenzyme M reductase (MCR), which plays a key role in CC methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- CC dependent amidation of the two carboxylate groups at positions a and c CC of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen CC source. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + CC cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate; CC Xref=Rhea:RHEA:26289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58537, ChEBI:CHEBI:58894, CC ChEBI:CHEBI:456216; EC=6.3.5.11; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + CC 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 CC phosphate; Xref=Rhea:RHEA:52896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:136841, CC ChEBI:CHEBI:136887, ChEBI:CHEBI:456216; EC=6.3.5.12; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): CC step 10/10. CC -!- DOMAIN: Comprises of two domains. The C-terminal domain contains the CC binding site for glutamine and catalyzes the hydrolysis of this CC substrate to glutamate and ammonia. The N-terminal domain is CC anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and CC catalyzes the ultimate synthesis of the diamide product. The ammonia CC produced via the glutaminase domain is probably translocated to the CC adjacent domain via a molecular tunnel, where it reacts with an CC activated intermediate. CC -!- MISCELLANEOUS: The a and c carboxylates of cobyrinate and Ni- CC sirohydrochlorin are activated for nucleophilic attack via formation of CC a phosphorylated intermediate by ATP. CbiA catalyzes first the CC amidation of the c-carboxylate, and then that of the a-carboxylate. else CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate CC groups at positions a and c of cobyrinate, using either L-glutamine or CC ammonia as the nitrogen source. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + CC cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate; CC Xref=Rhea:RHEA:26289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58537, ChEBI:CHEBI:58894, CC ChEBI:CHEBI:456216; EC=6.3.5.11; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): CC step 10/10. CC -!- DOMAIN: Comprises of two domains. The C-terminal domain contains the CC binding site for glutamine and catalyzes the hydrolysis of this CC substrate to glutamate and ammonia. The N-terminal domain is CC anticipated to bind ATP and cobyrinate and catalyzes the ultimate CC synthesis of the diamide product. The ammonia produced via the CC glutaminase domain is probably translocated to the adjacent domain via CC a molecular tunnel, where it reacts with an activated intermediate. CC -!- MISCELLANEOUS: The a and c carboxylates of cobyrinate are activated for CC nucleophilic attack via formation of a phosphorylated intermediate by CC ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then CC that of the a-carboxylate. end case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SIMILARITY: Belongs to the CobB/CbiA family. XX DR Pfam; PF01656; CbiA; 1; trigger=no DR Pfam; PF07685; GATase_3; 1; trigger=no DR NCBIfam; TIGR00379; CobB; 1; trigger=no DR PROSITE; PS51274; GATASE_COBBQ; 1; trigger=yes XX KW Cobalamin biosynthesis KW Glutamine amidotransferase KW ATP-binding KW Nucleotide-binding KW Ligase KW Magnesium case or or or KW Methanogenesis end case XX GO GO:0005524; F:ATP binding case or or or GO GO:0043802; F:hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) activity else GO GO:0042242; F:cobyrinic acid a,c-diamide synthase activity end case GO GO:0009236; P:cobalamin biosynthetic process XX FT From: COBB_SINSX (P21632) FT ACT_SITE 326 FT /note="Nucleophile" FT Condition: C FT SITE 426 FT /note="Increases nucleophilicity of active site Cys" FT Condition: H XX Size: 429-486; Related: MF_00028; Template: P29946; P21632; Q8TK00; Q46FL0; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.34 2023/06/01 //