ID   COBQ_METSB              Reviewed;         480 AA.
AC   B8EQG6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Msil_3272;
OS   Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS   13906 / BL2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2;
RX   PubMed=20472789; DOI=10.1128/jb.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK52179.1; -; Genomic_DNA.
DR   RefSeq; WP_012592248.1; NC_011666.1.
DR   AlphaFoldDB; B8EQG6; -.
DR   SMR; B8EQG6; -.
DR   STRING; 395965.Msil_3272; -.
DR   EnsemblBacteria; ACK52179; ACK52179; Msil_3272.
DR   KEGG; msl:Msil_3272; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_5; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002257; 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..480
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000201970"
FT   DOMAIN          246..434
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   480 AA;  49683 MW;  3BB776A8C583C022 CRC64;
     MIQGSGSDVG KSLIVAGLCR AYRNRGLKVL PFKPQNMSNN AAVTPDGGEI GRAQAMQALA
     CGAPLSVDMN PVLLKPQTGN GAQIVVQGKV VGTAAARDYQ QWKPKLLGAV LDSFSKLAAK
     ADLIVVEGAG SASEVNLRQN DIANMGFARA AGVPVILVGD IDRGGVIAQI VGTKSVIAPE
     DAAMIQGFII NKFRGDPTLF ADGMAFIAQR SGWPALGLIP FCAEAALLPA EDSFGLSTAR
     PKGRGKILIA VPILPGIANF DDLDPLRLEP DVEIAMVRSG EVLPAEARLV LLPGSKTTIA
     DLAAFRREGW DIDLAAHVRR GGHVIGLCGG YQMLGRTLRD PAGVEGPSGE AAGLGLLDVE
     TELTGDKTLA PAVGASAADG APFKGYEMHL GRTFGPGCAA PLLILADGRR EGAVSADGRV
     SGSYVHGLFS ELAQRASLLA RLGGEGSGLS YEASIERALD AVANHLESHM DLDHLLTLAS