ID   COBQ_GEOKA              Reviewed;         503 AA.
AC   Q5KZ06;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=GK1795;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76080.1; -; Genomic_DNA.
DR   RefSeq; WP_011231286.1; NC_006510.1.
DR   AlphaFoldDB; Q5KZ06; -.
DR   STRING; 235909.GK1795; -.
DR   EnsemblBacteria; BAD76080; BAD76080; GK1795.
DR   KEGG; gka:GK1795; -.
DR   PATRIC; fig|235909.7.peg.1922; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001172; 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..503
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141303"
FT   DOMAIN          255..444
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        436
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   503 AA;  55344 MW;  1CCF7DD381E541C7 CRC64;
     MAKALPIMFQ GTHSDAGKSV IATAFCRMFA QDGWKTAPFK SQNMSLNSYV TPDGNEIGRA
     QGIQAEAAGV AARAEMNPIL IKPSREHESQ IVVLGKPYGN MQAFAYRNEF FHQGLAVIRQ
     SLETLMNEYD RIVIEGAGSP AEVNLNDREL VNMRIARLAN APVVLIGDIE RGGVFASLVG
     TLSLLEPEDR KRVIGVIINK FRGDVALLKP GLDWFEQHTG VPVLGVVPYL PDLAIDAEDS
     LSLERFASSV GGEEAIDVAV IRCPKIANFT DIDPLLAEPD CRVRLVTHGD ELGAPDVIVL
     PGSKNTIEDL IYMKKRGLAS RIVSLVNEGK ARVVGLCGGY QMLGAVIRDP YGVETPLPEV
     KGLGLLPIET TLERTKITIR TEGMLTWAGE RFSVQGYEIH MGRSAPLPGY APLIEADGRH
     EGAKHSDERV LGTYMHDLFH NDAFRTAFFN NIRRQKGIAP SGVRLFRSLK EKAFDRLAAH
     VRQHVAVERI EQMMRQFGCR DHS