ID   COBQ_TRIV2              Reviewed;         491 AA.
AC   Q3MGR4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Ava_0196;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA19822.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MGR4; -.
DR   SMR; Q3MGR4; -.
DR   STRING; 240292.Ava_0196; -.
DR   EnsemblBacteria; ABA19822; ABA19822; Ava_0196.
DR   KEGG; ava:Ava_0196; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002533; 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..491
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332321"
FT   DOMAIN          250..441
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   491 AA;  54176 MW;  8178302E81DEB1CB CRC64;
     MKSIMVVGTT SHAGKSLIST AICRILSRRG WRVAPFKGQN MALNAYVTAN GGEIGYAQAV
     QAWAAGVVPW VEMNPILLKP QGDMTSQVII RGRPVGRVNA ADYYEQYFEP GWRAIEESLQ
     HLGTEFDLVV CEGAGSPAEI NLKHRDLTNM RVAKYLNAPT LLVVDIDRGG AFAHVVGTLE
     LLEPEERQLI KGVVINKFRG QRSLLDPGIK WLEERTGIPV VGVIPYLQEI FPAEDSLDLL
     ERKTHKAHAD LQITVVRLPR IANFTDFDPL ESEPTVAVKY ISPKQDLGHP DAVILPGTKT
     TIADLILLQK TGMAEAIQNY AASGGTVLGI CGGYQILGQM IADPEGIEGQ AGRYQGLNLL
     PIRTVITGQK IARQRQVSSN FPQLGLPVNG FEIHQGRSRV EPQGDSQAFQ PLFDDVNLGL
     VDSCQSVWGS YLHGLFDNGP WRRAWLNRLR QQRGLKSLPT GVANYREQRE QMLDNIATEV
     ENHLDLTLFL P