ID   COBQ_METTH              Reviewed;         504 AA.
AC   O26880;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Probable cobyric acid synthase;
GN   Name=cobQ; OrderedLocusNames=MTH_787;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB85289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000666; AAB85289.1; ALT_INIT; Genomic_DNA.
DR   PIR; B69205; B69205.
DR   RefSeq; WP_048061247.1; NC_000916.1.
DR   AlphaFoldDB; O26880; -.
DR   SMR; O26880; -.
DR   STRING; 187420.MTH_787; -.
DR   EnsemblBacteria; AAB85289; AAB85289; MTH_787.
DR   GeneID; 1471195; -.
DR   KEGG; mth:MTH_787; -.
DR   PATRIC; fig|187420.15.peg.774; -.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000005223; 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="Probable cobyric acid synthase"
FT                   /id="PRO_0000141352"
FT   DOMAIN          252..450
FT                   /note="GATase cobBQ-type"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        442
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   504 AA;  55831 MW;  8D4A8A35487A501E CRC64;
     MSAKCIMVQG TSSSAGKSVM VAALCRIFSR RGYRVAPFKS QNMSLNSFTT AENREIAVAQ
     VLQAEAAGIE PSHHMNPVLL KPKEDFTSQV IVHGRPAGNM NFQDYQTEFR DTALEAIRES
     LEYLKSRYEL IVIEGAGSPA EINMRDRDLA NMEIAHLADA DVILVADIDR GGVFASIAGT
     LMLLDERDRS RIKGVVINKF RGNIDILMPG IERIEEITGV PVLGVLPYDE GLKLPEEDSA
     SLSQRKYRGR GDIRVGVMRL PRISNFTDID PLEYEEDVAV RLIETGDSLD DLDAIIIPGT
     RNTISDLIHL EENGFADEIR DLSREIPVFG ICGGFQMLGK RILDDARQES SEGSVDGLGL
     LDCETHFTGE GKIISQSQGR VLGNGIFSGM RGETVEGYEL HEGTTVLGDV KPLLRVDRGF
     GNTRSGGFDG AVDGNVAGTY FHGIFHNFRF RRYFTNLLRE RKGIEPLEYL DDNFSASRRF
     SIDRLAEIVE ENMDLSIIEE ILEG