ID   COBQ_MOOTA              Reviewed;         517 AA.
AC   Q2RJH7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Moth_1098;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(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; CP000232; ABC19412.1; -; Genomic_DNA.
DR   RefSeq; WP_011392612.1; NC_007644.1.
DR   RefSeq; YP_429955.1; NC_007644.1.
DR   AlphaFoldDB; Q2RJH7; -.
DR   SMR; Q2RJH7; -.
DR   STRING; 264732.Moth_1098; -.
DR   PRIDE; Q2RJH7; -.
DR   EnsemblBacteria; ABC19412; ABC19412; Moth_1098.
DR   KEGG; mta:Moth_1098; -.
DR   PATRIC; fig|264732.11.peg.1179; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
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.
FT   CHAIN           1..517
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002367"
FT   DOMAIN          253..453
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        445
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   517 AA;  55616 MW;  C808DB3532C58A81 CRC64;
     MAKAIMLQGT SSNVGKSVLA AALCRIFHRN GYRVSPFKSQ NMALNSGATP DGGEMGRAQI
     VQAMAAGVVP RVEMNPILLK PTAHASSQVI VLGRPVGNLG AREYHGHFNQ KLWSRVEEAY
     AFLEREFEII VIEGAGSPAE INLKAGEIAN MRVARMAGAP VLLVADIDRG GALAAVVGTL
     ELLEPEERVM VAGIIINKFR GDLDLLKPAL DFLESRTGKP VLGVIPFLPD HGLPEEDSVV
     LEGVTGRSTG AGEVEIAVIK LPCISNFTDF DALEREKGVN LRYVEAASDL GNPDLVILPG
     SKNTIGDLLW LRCQGLETAI KELAGRGTPI IGICGGYQML GKEIRDPEHV ETDVEMIKGL
     DLLPIKTVFQ TSKATNQVRG VVTGSGPFLG PLQGQEVQGY EIHMGASFLL DGRPAFKITS
     RGGRLVTLDD GALAGEGRIW GTYIHGILDN DSLRHQVISV LRARRGLPAR PGMLNFMAEQ
     ERRLDILAGE VARHLDLGRL AAIMGLERPL VWTGHDN