ID B1VB59_CITFR Unreviewed; 459 AA. AC B1VB59; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 16-JAN-2019, entry version 54. DE RecName: Full=Cobyrinate a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027}; DE EC=6.3.5.11 {ECO:0000256|HAMAP-Rule:MF_00027}; DE AltName: Full=Cobyrinic acid a,c-diamide synthetase {ECO:0000256|HAMAP-Rule:MF_00027}; GN Name=cbiA {ECO:0000256|HAMAP-Rule:MF_00027, GN ECO:0000313|EMBL:CAM57280.1}; OS Citrobacter freundii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=546 {ECO:0000313|EMBL:CAM57280.1}; RN [1] {ECO:0000313|EMBL:CAM57280.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18332146; DOI=10.1074/jbc.M709214200; RA Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., RA Heldt D., Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., RA Bleloch A., McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., RA Prentice M.B.; RT "Biochemical and Structural Insights into Bacterial Organelle Form and RT Biogenesis."; RL J. Biol. Chem. 283:14366-14375(2008). CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two CC carboxylate groups at positions a and c of cobyrinate, using CC either L-glutamine or ammonia as the nitrogen source. CC {ECO:0000256|HAMAP-Rule:MF_00027}. 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 CC phosphate; Xref=Rhea:RHEA:26289, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:58537, CC ChEBI:CHEBI:58894, ChEBI:CHEBI:456216; EC=6.3.5.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00027}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00027}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 10/10. {ECO:0000256|HAMAP-Rule:MF_00027}. CC -!- DOMAIN: Comprises of two domains. The C-terminal domain contains CC the binding site for glutamine and catalyzes the hydrolysis of CC this 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 CC via a molecular tunnel, where it reacts with an activated CC intermediate. {ECO:0000256|HAMAP-Rule:MF_00027}. CC -!- MISCELLANEOUS: The a and c carboxylates of cobyrinate are CC activated for nucleophilic attack via formation of a CC phosphorylated intermediate by ATP. CbiA catalyzes first the CC amidation of the c-carboxylate, and then that of the a- CC carboxylate. {ECO:0000256|HAMAP-Rule:MF_00027}. CC -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000256|HAMAP- CC Rule:MF_00027}. 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; AM498294; CAM57280.1; -; Genomic_DNA. DR ProteinModelPortal; B1VB59; -. DR UniPathway; UPA00148; UER00231. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0043775; F:cobyrinate a,c-diamide synthase activity; IEA:UniProtKB-EC. DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00027; CobB_CbiA; 1. DR InterPro; IPR004484; CbiA_synth. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017929; CobB/CobQ_GATase. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR011698; GATase_3. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR43873; PTHR43873; 1. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF07685; GATase_3; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00379; cobB; 1. DR PROSITE; PS51274; GATASE_COBBQ; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00027}; KW Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00027, KW ECO:0000256|PROSITE-ProRule:PRU00606}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00027, KW ECO:0000256|PROSITE-ProRule:PRU00606, ECO:0000256|SAAS:SAAS00035243}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00027}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00027}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00027}. FT DOMAIN 252 446 GATase cobBQ-type. {ECO:0000259|PROSITE: FT PS51274}. FT ACT_SITE 334 334 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_00027}. FT SITE 438 438 Increases nucleophilicity of active site FT Cys. {ECO:0000256|HAMAP-Rule:MF_00027}. SQ SEQUENCE 459 AA; 49782 MW; D381FE981936382E CRC64; MAANFHAFVL AGTGSGCGKT TVTLGLLSLL KKRGLRVQPC KVGPDYLDTG WHTAVCGTAS RNLDSFMLPV PTLNALFREH MQHADIAVIE GVMGLYDGYG TDPNYCSTAA MAKQLGCPVI LLVDGKAVST SIAATVMGFQ HFDPTLNIAG VIVNRVNSET HYQLLKVAIE RYCAVPVLGY VPRMAGVALP ERHLGLVTAR ESVINQQPWQ AFAATLEQTL DIDALLRLSQ LDTLPAGEWP ALPAADAGAG LTLAIADDEA FNFYYPDNIT LLERTGLKIV RFSPLHDTCL PDCQMIWLGG GYPELHAAAL ARNIAMLNQL RAAHQQGVAI YAECGGLMYL GSSLEDSQGD TWLMADIIPG HSKMGKRLTR FGYCEAQAAQ QTLLAAEGEV LRGHEFHYSD FTPETPAVMN CRKVRDGKTL QAWSGGWQVG NTFASYLHVH FAQRPQMLNH WLAAARSAL //