ID COBQ_MYCTU Reviewed; 494 AA. AC P9WP95; L0T2Z2; O53677; P0A532; DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 1. DT 12-AUG-2020, entry version 32. DE RecName: Full=Cobyric acid synthase; GN Name=cobQ; Synonyms=cbiP; OrderedLocusNames=Rv0255c; ORFNames=MTV034.21c; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., RA Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the complete RT genome sequence."; RL Nature 393:537-544(1998). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.m111.011627; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution RT mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, CC and one molecule of ATP is hydrogenolyzed for each amidation (By CC similarity). {ECO:0000250}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily. CC {ECO:0000305}. 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; AL123456; CCP42984.1; -; Genomic_DNA. DR PIR; C70940; C70940. DR RefSeq; WP_003899877.1; NZ_NVQJ01000001.1. DR RefSeq; YP_177703.1; NC_000962.3. DR STRING; 83332.Rv0255c; -. DR PaxDb; P9WP95; -. DR PRIDE; P9WP95; -. DR EnsemblBacteria; CCP42984; CCP42984; Rv0255c. DR GeneID; 23493657; -. DR GeneID; 886673; -. DR KEGG; mtu:Rv0255c; -. DR KEGG; mtv:RVBD_0255c; -. DR TubercuList; Rv0255c; -. DR eggNOG; COG1492; Bacteria. DR KO; K02232; -. DR OMA; QVIIHGR; -. DR PhylomeDB; P9WP95; -. DR BioCyc; MTBH37RV:G185E-4377-MONOMER; -. DR UniPathway; UPA00148; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0015420; F:ATPase-coupled vitamin B12 transmembrane transporter activity; IEA:UniProtKB-UniRule. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR CDD; cd01750; GATase1_CobQ; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00028; CobQ; 1. 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; IPR033949; CobQ_GATase1. DR InterPro; IPR004459; CobQ_synth. DR InterPro; IPR011698; GATase_3. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF07685; GATase_3; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00313; cobQ; 1. DR PROSITE; PS51274; GATASE_COBBQ; 1. PE 1: Evidence at protein level; KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome. FT CHAIN 1..494 FT /note="Cobyric acid synthase" FT /id="PRO_0000141312" FT DOMAIN 253..432 FT /note="GATase cobBQ-type" FT ACT_SITE 334 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 424 FT /evidence="ECO:0000250" SQ SEQUENCE 494 AA; 52135 MW; D97858AA7BB56CA2 CRC64; MSGLLVAGTT SDAGKSAVTA GLCRALARRG VRVAPFKAQN MSNNSMVCRG PDGTGVEIGR AQWVQALAAR TTPEAAMNPV LLKPASDHRS HVVLMGKPWG EVASSSWCAG RRALAEAACR AFDALAARYD VVVAEGAGSP AEINLRAGDY VNMGLARHAG LPTIVVGDID RGGVFAAFLG TVALLAAEDQ ALVAGFVVNK FRGDSDLLAP GLRDLERVTG RRVYGTLPWH PDLWLDSEDA LDLQGRRAAG TGARRVAVVR LPRISNFTDV DALGLEPDLD VVFASDPRAL DDADLIVLPG TRATIADLAW LRARDLDRAL LVHVAAGKPL LGICGGFQML GRVIRDPYGI EGPGGQVTEV EGLGLLDVET AFSPHKVLRL PRGEGLGVPA SGYEIHHGRI TRGDTAEEFL GGARDGPVFG TMWHGSLEGD ALREAFLRET LGLAPSGSCF LAARERRLDL LGDLVERHLD VDALLNLARH GCPPTLPFLA PGAP //