ID   COBQ_SYNR3              Reviewed;         493 AA.
AC   A5GUP3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN   OrderedLocusNames=SynRCC307_1699;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-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; CT978603; CAK28602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5GUP3; -.
DR   SMR; A5GUP3; -.
DR   STRING; 316278.SynRCC307_1699; -.
DR   EnsemblBacteria; CAK28602; CAK28602; SynRCC307_1699.
DR   KEGG; syr:SynRCC307_1699; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001115; 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..493
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332396"
FT   DOMAIN          255..441
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        336
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   493 AA;  53928 MW;  A81D623B9B90DF74 CRC64;
     MTPPTPLMVL GTSSGAGKSL MTAALCRVLK RRGEQPLPFK GQNMSNNAWV DQSGGEMAYS
     QALQSWAAGL EPNCAMNPVL LKPQGNSTSE VIHGGESVGM ARAETYYQEW FKPGWLAIRQ
     GLEQLRQQHP HGRLVLEGAG SPVEVNLQHR DLTNLRLAQY LRARCLLVAD IERGGVFAQL
     VGTLQLLRPV ERPLVKGLLI NRFRGRQELF DPGVSWLSDN TGVPVLGVMP WLDELFPPED
     SLDLLERRGR KANAELEIAV LRLPSLSNFS DLDPLEAEPS VQLRWVQPGE ALGQPDAVVL
     PGSKQTLRDL KALQASGLAR ELQRFSAGGG AVLGICGGLQ MLGRELLDPD GLEGAAGASA
     AGLNLLPLQT RFGGSKALRQ RQAVAHWPTA ESCPIEGFEL HRGSTIALEP LQALCQEEGL
     GWVQGQVAGS YLHGLLENGR WRRQWLNQLR RRKQLPELAE DQGHHSLQRE ELLDRLADAF
     EANVDLTPLI SDP