ID   COBQ_RUMCH              Reviewed;         514 AA.
AC   B8I0R5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Ccel_1284;
OS   Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10) (Clostridium cellulolyticum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=394503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) 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; CP001348; ACL75640.1; -; Genomic_DNA.
DR   RefSeq; WP_015924789.1; NC_011898.1.
DR   AlphaFoldDB; B8I0R5; -.
DR   SMR; B8I0R5; -.
DR   STRING; 394503.Ccel_1284; -.
DR   EnsemblBacteria; ACL75640; ACL75640; Ccel_1284.
DR   KEGG; cce:Ccel_1284; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001349; 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..514
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000116902"
FT   DOMAIN          249..448
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   514 AA;  56500 MW;  397E78BB38795A45 CRC64;
     MAKPIMIQGT MSNAGKSLLT AGLCRIFTQD GYRVAPFKSQ NMALNSYITT DGSEMGRAQV
     VQAEAAGKAP DVRMNPILLK PTSEKGSQVI LGGKPIGNMT TTEYYAHKHN LLPHIKRAYE
     SLSQENDIIV IEGAGSPAEI NLKRDDFVNM GLAKMLKAPV LIAGDIDRGG VFASLYGTVM
     LFDEDERKHV KGTIINKFRG DVEILKPGLD MLCDLIHVPV VGVVPYLHVD IDDEDSLSER
     FSKKGPLGLI DIAVIKLPRI SNFTDFNALE HIECASVRYV SGTNELGNPD LIIIPGSKNT
     MGDLKWMREN GLEVCIKKHA AKNKPVFGIC GGYQMLCENL GDPYGVEHGG EMKGMGLLKS
     TTVFEKEKTR TRVMGTFSKV GGIFNGLSGK TFEGYEIHMG YTASEEGNEG DSSLSNLAEI
     SGNEKPDGMQ KGNVYGTYVH GVFDNDEILS EIAAALMKEK GLEYEKHTFF NLKEYKEKQY
     NLLADALREC LDMEYIYKVI EEGIENGNNE TNGY