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 07-SEP-2016, entry version 75. 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}; GN OrderedLocusNames=rrnAC1102; OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM OS B-1809) (Halobacterium marismortui). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; 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., RA Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., RA Date S.V., Marcotte E., Hood L., Ng W.V.; RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from RT the Dead Sea."; RL Genome Res. 14:2221-2234(2004). 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:0000255|HAMAP-Rule:MF_00027}. CC -!- CATALYTIC ACTIVITY: 2 ATP + cobyrinate + 2 L-glutamine + 2 H(2)O = CC 2 ADP + 2 phosphate + cobyrinate a,c-diamide + 2 L-glutamate. CC {ECO:0000255|HAMAP-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 CC route): step 10/10. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00027}. CC -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000255|HAMAP- CC Rule:MF_00027}. CC -!- SIMILARITY: Contains 1 GATase cobBQ-type domain. CC {ECO:0000255|HAMAP-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; NC_006396.1. DR ProteinModelPortal; Q5V341; -. DR STRING; 272569.rrnAC1102; -. DR EnsemblBacteria; AAV46061; AAV46061; rrnAC1102. DR GeneID; 3129257; -. DR KEGG; hma:rrnAC1102; -. DR eggNOG; arCOG00106; Archaea. DR eggNOG; COG1797; LUCA. DR HOGENOM; HOG000289959; -. DR KO; K02224; -. DR OMA; HTFHHST; -. DR BioCyc; HMAR272569:GJDH-991-MONOMER; -. DR UniPathway; UPA00148; UER00231. DR Proteomes; UP000001169; Chromosome I. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. 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 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; Cobalamin biosynthesis; Complete proteome; KW Glutamine amidotransferase; Ligase; Magnesium; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 439 Cobyrinate a,c-diamide synthase. FT /FTId=PRO_0000141274. FT DOMAIN 237 428 GATase cobBQ-type. {ECO:0000255|HAMAP- FT Rule:MF_00027}. FT ACT_SITE 317 317 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00027}. FT SITE 420 420 Increases nucleophilicity of active site FT Cys. {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 //