COBQ_MYCBP
ID COBQ_MYCBP Reviewed; 494 AA.
AC A1KF76;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BCG_0293c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; AM408590; CAL70277.1; -; Genomic_DNA.
DR RefSeq; WP_003899877.1; NC_008769.1.
DR AlphaFoldDB; A1KF76; -.
DR KEGG; mbb:BCG_0293c; -.
DR HOGENOM; CLU_019250_2_2_11; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001472; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 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; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
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 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase.
FT CHAIN 1..494
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332348"
FT DOMAIN 253..432
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
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
