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COBQ_METM5
ID   COBQ_METM5              Reviewed;         492 AA.
AC   A4FWW2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=MmarC5_0375;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-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; CP000609; ABO34691.1; -; Genomic_DNA.
DR   RefSeq; WP_011868146.1; NC_009135.1.
DR   AlphaFoldDB; A4FWW2; -.
DR   STRING; 402880.MmarC5_0375; -.
DR   EnsemblBacteria; ABO34691; ABO34691; MmarC5_0375.
DR   GeneID; 4928436; -.
DR   KEGG; mmq:MmarC5_0375; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 34382at2157; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000253; 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.
FT   CHAIN           1..492
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_1000002364"
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;  54775 MW;  BCA36D27DEA5BA1E CRC64;
     MAKFIMVVGT SSNSGKTVLV SGICRMLSNK GYKVAPFKSQ NMSLNSRVSI EDGEIAVAQY
     TQAMAARSEP SVHFNPILLK PKGNFVSQVI VHGIPYEDRD YNEYRSKKDD FLDKIKQSIN
     YLDKNYDYVV IEGAGSCCEI NLLKDDIANL RVAEIAGADA ILVSDIDRGG VFASIYGTVQ
     LLPENWRNLL KGFVINKFRG NIDVLKDGFE KIEELTKIPV IGTILYDETL ILPEEDSQAL
     EGKRVFGNVK SPIEVNIVKF SKIANFTDVD PLSSDCLMKY IDFNDDITGD ILILPGTRCS
     TVEMDLMKKH GLDKKILEFV ENGGIVLGIC GGYQTLGKML IDEDFSEGDI GTISGLGLFD
     METTFGNEKA IKNSTGTISI FDQNFNVTGY ELHEGHSVSN ETPLISLSRG FGNCGDSYDG
     SFKIIGNSYI FGTYFHGILE NFEFRNYLVN FVRHKKNLSK IENDNYAEIF NENMDKLSKL
     VEESLDLSKI IK
 
 
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