ID   COBQ_AZOSB              Reviewed;         492 AA.
AC   A1KBC7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, 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=azo3517;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL96133.1; -; Genomic_DNA.
DR   RefSeq; WP_011767239.1; NC_008702.1.
DR   AlphaFoldDB; A1KBC7; -.
DR   SMR; A1KBC7; -.
DR   STRING; 62928.azo3517; -.
DR   EnsemblBacteria; CAL96133; CAL96133; azo3517.
DR   KEGG; azo:azo3517; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_4; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002588; 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..492
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002344"
FT   DOMAIN          253..441
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   492 AA;  51818 MW;  A6652476E573206D CRC64;
     MSKASALMVQ GTTSDAGKST LVAGLARALV RRGVRVAPFK PQNMALNSAV TADGGEIGRA
     QALQAVAARI APHTDFNPVL LKPSSDIGAQ VIIHGKVMAN LSARDYHAYK PTAMAAVMAS
     FDRLSAQYEH VLIEGAGSPA EINLRDRDIA NMGFAEAADV PVVLVADIDR GGVFAHLVGT
     LELLSPSEQA RVRGFVINRF RGDIALLQPG LDWLTERTGR PVFGVLPYLH GLFLDAEDAL
     ANGQVAADRD GAVLKVIAPV YPRISNHTDL DALRLHPQVD FRWVGPGQAI PPADLVVLPG
     SKSVQADLAW LRAQGWEPAL RRHLRYGGKV IGICGGFQML GSTLADPHGL EGAPSTVAGL
     GALDIETVLE REKQLVNVRG RLALDGEAAV AGYEIHMGVS RGADLDRPAV LLEDGRADGA
     LSADGQVLGT YLHGLFDTPQ AVAALLDWAG LKGAAGVDLN ARREADLDRL ADAVEAHVDM
     AALFGAAWPD AA