ID CBIA_HALMA Reviewed; 439 AA. AC Q5V341; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 08-NOV-2023, entry version 101. DE RecName: Full=Cobyrinate a,c-diamide synthase {ECO:0000255|HAMAP-Rule:MF_00027}; DE EC=6.3.5.11 {ECO:0000255|HAMAP-Rule:MF_00027}; DE AltName: Full=Cobyrinic acid a,c-diamide synthetase {ECO:0000255|HAMAP-Rule:MF_00027}; GN Name=cbiA {ECO:0000255|HAMAP-Rule:MF_00027}; OrderedLocusNames=rrnAC1102; OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM OS B-1809) (Halobacterium marismortui). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Haloarculaceae; Haloarcula. OX NCBI_TaxID=272569; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=15520287; DOI=10.1101/gr.2700304; RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., RA Hood L., Ng W.V.; RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the RT Dead Sea."; RL Genome Res. 14:2221-2234(2004). 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:0000255|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:0000255|HAMAP- CC Rule:MF_00027}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00027}. CC -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000255|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; AY596297; AAV46061.1; -; Genomic_DNA. DR RefSeq; WP_011223446.1; NZ_CP039138.1. DR AlphaFoldDB; Q5V341; -. DR SMR; Q5V341; -. DR STRING; 272569.rrnAC1102; -. DR PaxDb; 272569-rrnAC1102; -. DR EnsemblBacteria; AAV46061; AAV46061; rrnAC1102. DR GeneID; 40152109; -. DR KEGG; hma:rrnAC1102; -. DR PATRIC; fig|272569.17.peg.1827; -. DR eggNOG; arCOG00106; Archaea. DR HOGENOM; CLU_022752_2_0_2; -. DR OMA; QPFKCGP; -. DR UniPathway; UPA00148; UER00231. DR Proteomes; UP000001169; Chromosome I. 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-KW. 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; 1. 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; Cobalamin biosynthesis; Glutamine amidotransferase; Ligase; KW Magnesium; Nucleotide-binding; Reference proteome. FT CHAIN 1..439 FT /note="Cobyrinate a,c-diamide synthase" FT /id="PRO_0000141274" FT DOMAIN 237..428 FT /note="GATase cobBQ-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00027" FT REGION 214..235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 317 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00027" FT SITE 420 FT /note="Increases nucleophilicity of active site Cys" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00027" SQ SEQUENCE 439 AA; 46284 MW; F49FFAFC63D97D5C CRC64; MEGFVLAGTS SGVGKTVATL ATLTALEDAG YQPQPAKAGP DFIDPSHHEA LVDTPSRTLD PWLAGEDGMR RTYWRGTGDI CVVEGVMGLY DGTKTSTAAV AEGLDLPVVL VVDAKAGMES VAATALGFAQ YADRIGVDIE VAGILAQRAH GGRHADGIRD ALPEDLTYFG RIPPMSDLEI PDRHLGLHMG SEAGLDRDAL STAAETIDIE RLVETARAPP EVATTERNTG DSPADRRVAV AQDSAFCFIY PSVLERLRSE ASVEPFSPVA GDSVPDADAI YLPGGYPELH GESLETGGTL DEIAVRAADG VPVYGECGGL MALSESLTTT DGDTYEMAGV LPADIEMQDR YQALDHVELE ARADTVAATS GAHRRGHEFH YSAATLGSDA SFAFDMVRGD GIDGEHDGLT EYSTIGTYCH CHGESGAFDR LLAVPSKDI //