ID   COBQ_SYNSC              Reviewed;         498 AA.
AC   Q3ALJ7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, 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};
GN   OrderedLocusNames=Syncc9605_0766;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-2005) 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; CP000110; ABB34535.1; -; Genomic_DNA.
DR   RefSeq; WP_011363761.1; NC_007516.1.
DR   AlphaFoldDB; Q3ALJ7; -.
DR   SMR; Q3ALJ7; -.
DR   STRING; 110662.Syncc9605_0766; -.
DR   EnsemblBacteria; ABB34535; ABB34535; Syncc9605_0766.
DR   KEGG; syd:Syncc9605_0766; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
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..498
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332392"
FT   DOMAIN          257..447
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        338
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        439
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   498 AA;  54484 MW;  C198B5A41EC78570 CRC64;
     MTGASPRPLM VLGTSSGAGK SLMTAALCRV LQRRGEQALP FKGQNMSNNA WVDADGGEMA
     YSQAMQAWAA GLEPCCSMNP VLLKPRGDST SEVIHGGQSV GIARAEHYYR DWFRPGWKAI
     RTGLMQLQQQ WPQGRLVLEG AGSPVEVNLQ RRDLTNLRLA QYLRANCLLV ADIERGGVFA
     QIVGTLSLLR PVESPLIKGI LINRFRGRRE LFDEGRRWLE ANTGVPVLGV MPWLNELFPP
     EDSLDLLERK PTRGATDLEI AVLRLPSLSN FSDLDPLEAE ASLRLRWIQP GEPLGEPDAV
     ILPGSKQTLR DLEAMNSCGL ADQLRAYAQA GGSVLGICGG MQMLGRSLSD PEGLEGTDQR
     CSQNGLGLLP LETTFSGTKR LSQRSIDGLW PMETPLSGFE LHYGTTIPDA GLQPLSSDPG
     LGWWAPGPKG SSVVGTYLHG LLDNGPWRRA WLNRLREQRG LQPLANDPKN HSAHRDLLLD
     RLADAFEQHV NLAPLLQP