ID   COBQ_LIMRD              Reviewed;         501 AA.
AC   A5VM70;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Lreu_1705;
OS   Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA   Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(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.
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; CP000705; ABQ83944.1; -; Genomic_DNA.
DR   RefSeq; WP_003669125.1; NZ_AZDD01000019.1.
DR   AlphaFoldDB; A5VM70; -.
DR   SMR; A5VM70; -.
DR   STRING; 557436.Lreu_1705; -.
DR   PRIDE; A5VM70; -.
DR   EnsemblBacteria; ABQ83944; ABQ83944; Lreu_1705.
DR   GeneID; 66471882; -.
DR   KEGG; lre:Lreu_1705; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001991; 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; 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; 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; Reference proteome.
FT   CHAIN           1..501
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332344"
FT   DOMAIN          252..443
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   501 AA;  55166 MW;  94707624FF74D0A6 CRC64;
     MTVQSIMFQG TASDAGKSWL AAAVCRILAN RGQKVAPFKS QNMALNSFIT EKGDEMGRAQ
     VFQAEAAKVK PDVRMNPILL KPSTDKDSQV IVMGKVLKNM DAVSYYQFKR ELIPQIMMAY
     NTLADENDVI VLEGAGSPAE INLNENDIVN MGMARMADAP VILVADIDKG GVFASIYGTI
     KLMPREDQQR IKGIIINKFR GDKSLLESGN KMIEKLTGIP VIGVLPMSSI DIDEEDSVSL
     IRKPRQKDTQ KDLDVAVIDL DKISNFTDIH SLEIQPDVSV RYVLTAEELG TPDLLIIPGS
     KNTNADLVAL RKNGIAEGIL RAHKDGSMIV GICGGYQILG QMLYDPTGIE SPIKEQKGLG
     LLDTETTFNE KKTTTQAVAK RNNYILKGYE IHMGTTKRGL NSTPFSTIQE TNGQPENRED
     GAVSTDGTVI GTYLHGIFDN PYWTRHLLNQ LRVAKGMAPL VDTTVSISGY KDQQYEKLAQ
     LFAQNVDMDK FNQILQDSTK E