ID B1VB59_CITFR Unreviewed; 459 AA. AC B1VB59; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 13-SEP-2023, entry version 67. 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; Pseudomonadota; 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., Heldt D., RA Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A., RA McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., 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 carboxylate CC groups at positions a and c of cobyrinate, using either L-glutamine or CC ammonia as the nitrogen source. {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 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00027}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_00027}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): CC step 10/10. {ECO:0000256|HAMAP-Rule:MF_00027}. 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 {ECO:0000256|HAMAP-Rule:MF_00027}. 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. {ECO:0000256|HAMAP-Rule:MF_00027}. CC -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000256|HAMAP- CC Rule:MF_00027}. CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily. CC {ECO:0000256|ARBA:ARBA00006205}. 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 AlphaFoldDB; B1VB59; -. DR UniPathway; UPA00148; UER00231. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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 CDD; cd05388; CobB_N; 1. DR CDD; cd03130; GATase1_CobB; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR HAMAP; MF_00027; CobB_CbiA; 1. DR InterPro; IPR004484; CbiA_synth. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR011698; GATase_3. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00379; cobB; 1. DR PANTHER; PTHR43873; COBYRINATE A,C-DIAMIDE SYNTHASE; 1. DR PANTHER; PTHR43873:SF1; COBYRINATE A,C-DIAMIDE SYNTHASE; 1. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF07685; GATase_3; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|HAMAP-Rule:MF_00027}; 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 9..194 FT /note="CobQ/CobB/MinD/ParA nucleotide binding" FT /evidence="ECO:0000259|Pfam:PF01656" FT DOMAIN 253..444 FT /note="CobB/CobQ-like glutamine amidotransferase" FT /evidence="ECO:0000259|Pfam:PF07685" FT ACT_SITE 334 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00027" FT SITE 438 FT /note="Increases nucleophilicity of active site Cys" FT /evidence="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 //