ID   COBQ_ACIAC              Reviewed;         492 AA.
AC   A1TMF3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Aave_1552;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) 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; CP000512; ABM32141.1; -; Genomic_DNA.
DR   RefSeq; WP_011794689.1; NC_008752.1.
DR   AlphaFoldDB; A1TMF3; -.
DR   STRING; 397945.Aave_1552; -.
DR   PRIDE; A1TMF3; -.
DR   EnsemblBacteria; ABM32141; ABM32141; Aave_1552.
DR   KEGG; aav:Aave_1552; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_1_4; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002596; 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_0000332316"
FT   DOMAIN          259..453
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        340
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        445
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   492 AA;  52084 MW;  7A651CA7F6815AF2 CRC64;
     MIARCIMVLG TSSGAGKSWL ATALCRWFSD QGLRVAPFKA QNMSNNARVV AAPGGGQGEI
     GSAQYFQALA ARTEPEVRMN PVLLKPEADT RSQVVLMGQV SEELTRMPWR GRSVHVWPHV
     AAALDALRAE NDVVVIEGAG SPAEINLHAN DIVNMRVARH AGAHGLLVTD IDRGGAFAHL
     YGTWALLPED ERALIQGFVL NKFRGDAALL APAPDMLRER TGVPTVATIP MQWRHGLPEE
     DGVFDDAGHV RAGAGGAVHT TVAVVAYPRI SNLDEFQPLK GVPGLRLVWA RSPAEVAGAD
     WIVLPGSKAT AADLAWLRAQ GLDAAIAAHA ARGGRVLGIC GGLQMLGEAL IDTHGVDGNA
     PGLGLLPLVT AFDPAKTVRR TRTAFGALRG AWSALSGVAV QGYEIRHGRT AQHPAMAAAG
     DVAHPAIPGL AWQNARGNVL GLYLHGLFED AVALRALFGA DVPTLDAVFD RLARGVDEWF
     DPAWRAARRA GR