ID   COBQ_GRABC              Reviewed;         481 AA.
AC   Q0BUF0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN   OrderedLocusNames=GbCGDNIH1_0654;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61552.1; -; Genomic_DNA.
DR   RefSeq; WP_011631361.1; NC_008343.2.
DR   AlphaFoldDB; Q0BUF0; -.
DR   SMR; Q0BUF0; -.
DR   STRING; 391165.GbCGDNIH1_0654; -.
DR   EnsemblBacteria; ABI61552; ABI61552; GbCGDNIH1_0654.
DR   KEGG; gbe:GbCGDNIH1_0654; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_5; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001963; 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..481
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332339"
FT   DOMAIN          248..435
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        329
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   481 AA;  50364 MW;  A3D5038AFFADCD4C CRC64;
     MIQGTGSSVG KSLLVAGVSR ALTRRGLVVR PFKPQNMSNN AAIAADGGEI GRAQALQARA
     CRISPSHHMN PVLLKPQSEI GAQIVVQGKV HGQATARAYQ AMKPQLLGTV LESFGILRKQ
     ADIVLVEGAG SASEINLRAG DIANMGFARA ANVPVVIAGD IDRGGVIAAL VGTKTVLDPD
     DAAMVRGFLV NRMRGDPSLF AEGMRLIEQQ TGWEALGLVP HCEAARALPA EDAADLLRGL
     SAPTRSGNTV IAVPMLPHIA NFDDLDPLAA EDSVTLVMVP PGQPLPVADA IIIPGSKTVI
     ADLAALRHHG WDIDILAHRR RGRSIIGLCG GYQMLGRAIH DPQGFEGPAG SAAGLGLLEI
     ETVLEPHKIL TSRSGHLFNH DVPVSGYEMH MGITTGSGLR RPLLSLGPDA PEGCVSADGV
     VMGTYLHGLF HGGAFRRHLL ATLDVSSHGG DHEDAVEHAL DALADHMEAH VAIDRLLALS
     A