ID   COBQ_METM6              Reviewed;         492 AA.
AC   A9AA97;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=MmarC6_1457;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX02270.1; -; Genomic_DNA.
DR   RefSeq; WP_012194190.1; NC_009975.1.
DR   AlphaFoldDB; A9AA97; -.
DR   STRING; 444158.MmarC6_1457; -.
DR   PRIDE; A9AA97; -.
DR   EnsemblBacteria; ABX02270; ABX02270; MmarC6_1457.
DR   GeneID; 5737602; -.
DR   KEGG; mmx:MmarC6_1457; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 34382at2157; -.
DR   PhylomeDB; A9AA97; -.
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; 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.
FT   CHAIN           1..492
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_1000090233"
FT   DOMAIN          252..444
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        436
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   492 AA;  54756 MW;  AF2679E164982442 CRC64;
     MAKFIMVVGT SSNSGKTVLV SGICRMLSNK GYKVAPFKSQ NMSLNSRVSI EDGEIAVAQY
     TQAMAARAEP SIHFNPILLK PKGNFVSQVI VHGIPYEDRD YNEYRSKKDV LLEKIKESIE
     YLDKNYDYVV IEGAGSCCEI NLLKDDIANL RIAEISGADA ILVSDIDRGG VFAAIYGTVK
     LLPENWRKLL KGFVINKFRG NLDVLKDGFE KIEELTNIPV IGTIPYDETL ILPEEDSQAL
     EGKRVFGNVK SPIEVNIVKF SKIANFTDVD PLSSDCLMKY IDFNDDITGD ILILPGTRCS
     TVEMDLMKKH GMDKKIMEFV ENGGIVLGIC GGYQTLGKIL IDENFSEGDV GTISGLGLFD
     METTFGNKKA IKNSTGTISI FDQNFDVMGY ELHEGHSISN ETPLISLSRG FGNCGDSYDG
     SFKVIGDSYI FGTYFHGILE NFEFRNYLVN IVNNKKNLSR IENDNYAEIF NENMDKLSKL
     IEENLDLSKI IK