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 05-OCT-2016, entry version 16. DE RecName: Full=Cobyric acid synthase; GN Name=cobQ; Synonyms=cbiP; OrderedLocusNames=Rv0255c; GN 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., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete 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., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution 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 CC glutamine, and one molecule of ATP is hydrogenolyzed for each CC amidation (By similarity). {ECO:0000250}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GATase cobBQ-type domain. {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_KK339370.1. DR RefSeq; YP_177703.1; NC_000962.3. DR ProteinModelPortal; P9WP95; -. DR SMR; P9WP95; 1-239, 1-232, 2-344. DR STRING; 83332.Rv0255c; -. DR PaxDb; P9WP95; -. DR PRIDE; P9WP95; -. DR EnsemblBacteria; CCP42984; CCP42984; Rv0255c. DR GeneID; 886673; -. DR KEGG; mtu:Rv0255c; -. DR TubercuList; Rv0255c; -. DR eggNOG; ENOG4105CAA; Bacteria. DR eggNOG; COG1492; LUCA. DR KO; K02232; -. DR OMA; KRHLRYG; -. DR PhylomeDB; P9WP95; -. DR UniPathway; UPA00148; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0015420; F:cobalamin-transporting ATPase activity; IEA:UniProtKB-HAMAP. 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_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; IPR004459; CobQ_synth. 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; TIGR00313; cobQ; 1. DR PROSITE; PS51274; GATASE_COBBQ; 1. PE 1: Evidence at protein level; KW Cobalamin biosynthesis; Complete proteome; Glutamine amidotransferase; KW Reference proteome. FT CHAIN 1 494 Cobyric acid synthase. FT /FTId=PRO_0000141312. FT DOMAIN 253 432 GATase cobBQ-type. FT ACT_SITE 334 334 Nucleophile. {ECO:0000250}. FT ACT_SITE 424 424 {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 //