ID COBB_HALMA Reviewed; 439 AA. AC Q5V341; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 16-MAY-2012, entry version 49. DE RecName: Full=Probable cobyrinic acid A,C-diamide synthase; GN Name=cobB; 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: Responsible for the amidation of carboxylic groups at CC position A and C of either cobyrinic acid or hydrogenobrynic acid. CC NH(2) groups are provided by glutamine, and one molecule of ATP is CC hydrogenolyzed for each amidation (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobB subfamily. CC -!- SIMILARITY: Contains 1 GATase cobBQ-type domain. 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; YP_135767.1; NC_006396.1. DR ProteinModelPortal; Q5V341; -. DR GeneID; 3129257; -. DR GenomeReviews; AY596297_GR; rrnAC1102. DR KEGG; hma:rrnAC1102; -. DR eggNOG; COG1797; -. DR HOGENOM; HOG000289959; -. DR KO; K02224; -. DR OMA; EGMMGLY; -. DR ProtClustDB; PRK13896; -. DR BioCyc; HMAR272569:RRNAC1102-MONOMER; -. DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR HAMAP; MF_00027; CobB; 1; -. DR InterPro; IPR004484; CbiA_synth. DR InterPro; IPR017929; CobB/CobQ_GATase. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR011698; GATase_3. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF07685; GATase_3; 1. DR TIGRFAMs; TIGR00379; CobB; 1. DR PROSITE; PS51274; GATASE_COBBQ; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Glutamine amidotransferase. FT CHAIN 1 439 Probable cobyrinic acid A,C-diamide FT synthase. FT /FTId=PRO_0000141274. FT DOMAIN 237 428 GATase cobBQ-type. FT ACT_SITE 317 317 Nucleophile (By similarity). FT ACT_SITE 420 420 By similarity. 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 //