ID   COBQ_PSEA7              Reviewed;         490 AA.
AC   A6V8T2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PSPA7_4113;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-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; CP000744; ABR81534.1; -; Genomic_DNA.
DR   RefSeq; WP_012076593.1; NC_009656.1.
DR   AlphaFoldDB; A6V8T2; -.
DR   SMR; A6V8T2; -.
DR   EnsemblBacteria; ABR81534; ABR81534; PSPA7_4113.
DR   KEGG; pap:PSPA7_4113; -.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001582; 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..490
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332367"
FT   DOMAIN          252..439
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        431
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   490 AA;  52426 MW;  953E335C4FAD72E4 CRC64;
     MSDRGRTLMV QGTTSDAGKS TLVTALCRWL ARRGVAVAPF KPQNMALNSA VTADGGEIGR
     AQAVQAQACR LAPHTDMNPV LLKPNTDIGA QVIIHGRAVT SMDAAAYHDY KRVAMEAVLA
     SHARLAAAYR VVMVEGAGSP AEINLRANDI ANMGFAEAVD CPVILVADID RGGVFAHLVG
     TLELLSDSER ERVRGFVINR FRGDIALLQP GLDWLEARTG KPVLGVLPYV SDLHLEAEDA
     IDTRQAAKTG PRLKVVVPVL PRISNHTDFD PLRLHPQVEL SFVGPGQALP PADLIVLPGS
     KSVRADLAAL RERGWDEAIL RHLRYGGRLL GICGGLQMLG ERLHDPLGLE GAAGSSAGLG
     LLALETTLEA DKQLRNVQGR LSLEDAPLSG YEIHAGVTRG EALARPAVVL DDGRADGARS
     VDGNVMGTYL HGLFESTAAC SALLRWAGLR EVRAVDYQAL RERDIERLAD LVERHLDTGR
     LLALCGEPHA