ID   COBQ_METST              Reviewed;         502 AA.
AC   Q2NEZ9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Msp_1226;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57604.1; -; Genomic_DNA.
DR   RefSeq; WP_011406803.1; NC_007681.1.
DR   AlphaFoldDB; Q2NEZ9; -.
DR   SMR; Q2NEZ9; -.
DR   STRING; 339860.Msp_1226; -.
DR   EnsemblBacteria; ABC57604; ABC57604; Msp_1226.
DR   GeneID; 41325795; -.
DR   KEGG; mst:Msp_1226; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 34382at2157; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001931; 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..502
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_0000332406"
FT   DOMAIN          250..448
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   502 AA;  55995 MW;  3864DFCA0DA2E930 CRC64;
     MKYIMFQGTS SNAGKTLTVA ALCNLLSRKG YRVTPFKSQN MSLNSYTTVD NDEMSIAQVM
     QSEAAGIEPN CNMNPILLKP KEDFTSQVIV QGKPAGNMRF DDYQNNFRTQ AIKAIEESLE
     YLKEDYDITV IEGAGSPAEI NMYDKDLANM LIARMTDADV ILVADIDQGG VFASIVGTYF
     LIPEEDRKRI KAVIINKFRG NADVLKPGIE KIEELTNIPV IGIIPYDETL NLPEEDSASL
     STHHFSENEK ITIGTLRLPR ISNFTDIDPL DYEEDIGIKL VSIYDDLEDL DALIIPGTRN
     TVNDLVELKK SGAFDKIKKI SKEIPIFGIC GGYQMLSNNI IDESCSESKY GSVEGLGLLD
     MTTEFGQIEK VVQQSEGTII KDSSLGFEKD TKVTGYELHE GITILGDVEP LIKIKKGQGN
     DESGLYDGAI NGNVCGTYFH GIFHNFEFRR KFTDQLRINK GLKPLGLTKD DFKESKRVNY
     DQLGDLFANN VDMSFFKDLL RD