ID   COBQ_LIMRJ              Reviewed;         501 AA.
AC   B2G9H7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=LAR_1593;
OS   Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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}.
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; AP007281; BAG26109.1; -; Genomic_DNA.
DR   RefSeq; WP_003669125.1; NC_010609.1.
DR   AlphaFoldDB; B2G9H7; -.
DR   SMR; B2G9H7; -.
DR   GeneID; 66471882; -.
DR   KEGG; lrf:LAR_1593; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
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; 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.
FT   CHAIN           1..501
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000090231"
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