ID   COBQ_RUEST              Reviewed;         482 AA.
AC   Q1GF45;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=TM1040_1989;
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX   NCBI_TaxID=292414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
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; CP000377; ABF64721.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1GF45; -.
DR   SMR; Q1GF45; -.
DR   STRING; 292414.TM1040_1989; -.
DR   EnsemblBacteria; ABF64721; ABF64721; TM1040_1989.
DR   KEGG; sit:TM1040_1989; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_5; -.
DR   OMA; DVRMNPL; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000636; 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; 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; 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..482
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332387"
FT   DOMAIN          243..430
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        325
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   482 AA;  51028 MW;  3A9085DB7D20C924 CRC64;
     MIQGTGSNVG KSMLVAGLAR ALRKRGLSVA PFKPQNMSNN AAVTSDGGEI GRAQALQARA
     AGLAPHTDMN PVLLKPETDT GAQVIVQGKR RGTRAAGSFM RDKAGLLEAT LESFHRLAAQ
     HDIVLIEGAG SPAETNLRKG DIANMGFAEA AGVPVLLVGD IHRGGVIAQI VGTHTVLEPS
     DRARIKAFAV NRFRGDLSLF DGGRDDIARW TGWPSLGVVP WFWDAWKLPA EDMMDIASHK
     GGACKVVVPQ LERMANFDDL DPLAAEPAVT VEIVPPGRAL PGDADLVLIP GSKSTIGDLA
     YLRTQGWDID ILAHHRRGGH VLGLCGGYQM LGQSIDDPEG VDGHPGKVAG LGLLDVHTVM
     AGDKRVTLSA ARTLEGDLPV SGYEIHMGRT TGPDCARAWL ALEGRAEGAT SADGRVRGSY
     LHGLFTSDAF RAQFLSDLGH QSDLDYDAGV EATLDELAAH LEQYMDVEGL LELAEPIPVP
     ES