ID F0JHM7_PSEME Unreviewed; 462 AA. AC F0JHM7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 04-NOV-2026, entry version 76. 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 ORFNames=DND132_2058 {ECO:0000313|EMBL:EGB15263.1}; OS Pseudodesulfovibrio mercurii. OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia; OC Desulfovibrionales; Desulfovibrionaceae. OX NCBI_TaxID=641491 {ECO:0000313|EMBL:EGB15263.1, ECO:0000313|Proteomes:UP000007845}; RN [1] {ECO:0000313|EMBL:EGB15263.1, ECO:0000313|Proteomes:UP000007845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ND132 {ECO:0000313|EMBL:EGB15263.1, RC ECO:0000313|Proteomes:UP000007845}; RX PubMed=21357488; DOI=10.1128/JB.00170-11; RA Brown S.D., Gilmour C.C., Kucken A.M., Wall J.D., Elias D.A., Brandt C.C., RA Podar M., Chertkov O., Held B., Bruce D.C., Detter J.C., Tapia R., RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Woyke T., Mikhailova N., RA Ivanova N.N., Han J., Lucas S., Lapidus A.L., Land M.L., Hauser L.J., RA Palumbo A.V.; RT "Genome sequence of the mercury-methylating strain Desulfovibrio RT desulfuricans ND132."; RL J. Bacteriol. 193:2078-2079(2011). 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=cob(II)yrinate + 2 L-glutamine + 2 ATP + 2 H2O = CC cob(II)yrinate a,c diamide + 2 L-glutamate + 2 ADP + 2 phosphate + 2 CC H(+); 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, ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; CP003220; EGB15263.1; -; Genomic_DNA. DR RefSeq; WP_014322690.1; NC_016803.1. DR AlphaFoldDB; F0JHM7; -. DR SMR; F0JHM7; -. DR STRING; 641491.DND132_2058; -. DR KEGG; ddn:DND132_2058; -. DR eggNOG; COG1797; Bacteria. DR HOGENOM; CLU_022752_2_0_7; -. DR OrthoDB; 9764035at2; -. DR UniPathway; UPA00148; UER00231. DR Proteomes; UP000007845; Chromosome. 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:L-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/CobB_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 NCBIfam; NF002204; PRK01077.1; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00027}; KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP- KW Rule:MF_00027}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|HAMAP-Rule:MF_00027}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00027}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00027}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00027}; Reference proteome {ECO:0000313|Proteomes:UP000007845}. FT DOMAIN 9..199 FT /note="CobQ/CobB/MinD/ParA nucleotide binding" FT /evidence="ECO:0000259|Pfam:PF01656" FT DOMAIN 253..446 FT /note="CobB/CobQ-like glutamine amidotransferase" FT /evidence="ECO:0000259|Pfam:PF07685" FT ACT_SITE 336 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00027" FT SITE 440 FT /note="Increases nucleophilicity of active site Cys" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00027" SQ SEQUENCE 462 AA; 50239 MW; 3CF537C442590DAF CRC64; MVSAVKGFVI AGTHSGCGKT SISLGLMASL ARRGRRVQPF KCGPDFIDPG HHALACAVDG HPVPSHNLDG WMLDEATNLD LFNRYAAECD VAVIEGVMGL FDGISGTGDA GSTAQMAKIL GLPVILVVDA RSMARSAAAL VAGYADFDPA VTIAGVIFNR VGSPAHAELL REAMTLVPDV PVLGVLGRDE DISTPSRHLG LVTPEQDGPD MDRYQRLADW VETGLDPDAL LARLPEVEAV PPFEPVPQLP RVTIGLARDD AFCFYYEENL RLLREAGARL IEFSPLNDPH LPEHLDGLYL GGGYPELYVF ELGQNTRMRR DIKEFCESGR PVYAECGGFM LLMNDIITGR GRYAMAGVYP VRAEMNEKFR ALGYREITAR EATLLGPAGT TARGHEFHYS SIQDHDPELL HPVYAMAGRK GPLEEPEGFV TWNVLGSYVH LHFGSNPEIP KAFVKACMDV AR //