ID   COBQ_LACP7              Reviewed;         513 AA.
AC   A9KMP5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Cphy_1112;
OS   Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS   (Clostridium phytofermentans).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=357809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-2007) 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; CP000885; ABX41490.1; -; Genomic_DNA.
DR   RefSeq; WP_012199136.1; NC_010001.1.
DR   AlphaFoldDB; A9KMP5; -.
DR   SMR; A9KMP5; -.
DR   STRING; 357809.Cphy_1112; -.
DR   EnsemblBacteria; ABX41490; ABX41490; Cphy_1112.
DR   KEGG; cpy:Cphy_1112; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000370; 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; Reference proteome.
FT   CHAIN           1..513
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332334"
FT   DOMAIN          252..457
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        449
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   513 AA;  57081 MW;  66EB85EB488A09AE CRC64;
     MAKSIMIQGT MSSAGKSLLV TALCRILKQD GYKVAPFKSQ NMALNSFITE DGYEMGRAQV
     VQAEAAGIKP SVLMNPILLK PTTDVGSQVI VNGEVRGNMT ASNYFKYKKE LIPEIMHSYQ
     TLDKEYDIIV IEGAGSPAEI NLKSEDIVNM GMARMANAPV LLVGDIDRGG VFAQLYGTVA
     LLEEEERAMI KGMIINKFRG DVKILEPGLT MLSDRLSPIA NIPFVGVVPY TTVDIEEEDS
     ISERFLRKTA KKIDIAVIRL PRISNYTDFH NLERFPNVSV RYISKVSELL EPDMIILPGT
     KNTIDDLKFL RESGLEAAIL KAESKDTLIF GICGGYQMLG EWLHDPYGVE GGGEIKGLSL
     LPINTVFAKE KVRKQNSGTL NKVAGMLSGL SGKTYQGYEI HMGESTWSSK VEEEKNNCFS
     NKDEENLEHN TITSVLISNG AHVYGTYLHG IFDEEGICKE IIGTLCKRKG IDFEEVYEFD
     YKQYKEEQYD KLADAVRSSL DMKKIYQIME EGV