ID   COBQ_ANOFW              Reviewed;         504 AA.
AC   B7GLS9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Aflv_2170;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ34529.1; -; Genomic_DNA.
DR   RefSeq; WP_012575707.1; NC_011567.1.
DR   AlphaFoldDB; B7GLS9; -.
DR   SMR; B7GLS9; -.
DR   STRING; 491915.Aflv_2170; -.
DR   EnsemblBacteria; ACJ34529; ACJ34529; Aflv_2170.
DR   KEGG; afl:Aflv_2170; -.
DR   PATRIC; fig|491915.6.peg.2229; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000742; 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..504
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000116431"
FT   DOMAIN          254..442
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        434
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   504 AA;  56580 MW;  C3E9ABDDDA68EFE9 CRC64;
     MRRALPIMFQ GTHSDAGKSM LATAFCRIFA RNGWKTAPFK SQNMSLNSYV TLDGKEIGRA
     QGVQAEAAGV VATTHMNPIL IKPSRDQEAQ IVVHGKPYEN MKASTYRNEF FHLGLELIQQ
     SLHVLMNEYD RLVIEGAGSP AEVNLNDREL VNMRVARMAN APVVLVGDIE RGGVFASLVG
     TLQLLEEQDR KRVIGVIINK FRGDLSLLEP GLRWFEQYTG VKVLGVVPYM HVRIDAEDSV
     ALSRYATKKD DAKAIDVAVI RYPRISNFTD IDPFFAEPDC SVRFVSDASS LGEPDILILP
     GSKNTIEDVY FLTETGLFSS IQRLYERTNV TMIGICGGYQ MLGECIKDPF HVETPLDAVA
     GLSLLPIETT LACEKTTVLS EGTLVYKNEM FDVKGYEIHM GRSIVKQGEP LILLSGKTDG
     CKTKDERVIG TYMHDLFHND MFRHHLLNGV RRKKQLSPLM ERPNYRQLRA QAFDDLADCV
     EKHVDVKAIE RKMIEFQRGE HHAL