ID   COBQ_MYCSS              Reviewed;         495 AA.
AC   Q1BAC5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-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=Mmcs_2051;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000384; ABG08159.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1BAC5; -.
DR   SMR; Q1BAC5; -.
DR   KEGG; mmc:Mmcs_2051; -.
DR   HOGENOM; CLU_019250_2_2_11; -.
DR   OMA; EIHHGVA; -.
DR   BioCyc; MSP164756:G1G6O-2097-MON; -.
DR   UniPathway; UPA00148; -.
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..495
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332353"
FT   DOMAIN          258..427
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   495 AA;  52111 MW;  8CE6217C71FDFF75 CRC64;
     MTGGALLVAG TTSDAGKSMV VAGLCRLLAR KGVRVAPFKA QNMSNNSAVT VDGGEIGRAQ
     AMQARAAGLD PSVRFNPVLL KPGSDRTSQL VVRGRVTGTV SATDYITHRD RLADVVADEL
     ASLRAEFDVV LCEGAGSPAE INLRRTDLAN MGLARRAHLP VIVVGDIDRG GVLAHLFGTV
     AVLHPDDQAL IAGFVVNKFR GDPTLLAPGL DQLHDLTGRP TYGVIPYSDE LWMDTEDSVS
     VVAGRTIGRP TPPRGADGLR VAAVRLPRIS NSTDIEALAC EPGVTVRWVT DPADVADADV
     VVLPGTKATV ADLQWLRTAG LAEPIAAHAG AGRPLLGICG GFQMLCRHID DAVESRAGRV
     DGLGLLDADI AFAAEKTLRH RTTPLQGYEI HHGQVTRCAA DDWAGIGVRR DAVYGTHWHG
     LFDNDGFRRA WLADAAAAAG RSGFVVADDI DVSARRDAQL DVMADLLQNH LDLDAALGLV
     DAGPPPRPTI STGIT