ID   COBQ_THEKO              Reviewed;         483 AA.
AC   O33475; Q5JI00;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Probable cobyric acid synthase;
GN   Name=cobQ; OrderedLocusNames=TK0854;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RA   Rahman R., Fujiwara S., Imanaka T.;
RT   "Gene cloning and sequence analysis of cobyric acid synthase and cobalamin
RT   (5'-phosphate) synthase from hyperthermophilic archaeon Pyrococcus sp.
RT   KOD1.";
RL   J. Ferment. Bioeng. 83:109-112(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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}.
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DR   EMBL; D50533; BAA21090.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85043.1; -; Genomic_DNA.
DR   RefSeq; WP_011249805.1; NC_006624.1.
DR   AlphaFoldDB; O33475; -.
DR   SMR; O33475; -.
DR   STRING; 69014.TK0854; -.
DR   EnsemblBacteria; BAD85043; BAD85043; TK0854.
DR   GeneID; 3235931; -.
DR   KEGG; tko:TK0854; -.
DR   PATRIC; fig|69014.16.peg.833; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   InParanoid; O33475; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 34382at2157; -.
DR   PhylomeDB; O33475; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000536; 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..483
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_0000141356"
FT   DOMAIN          247..433
FT                   /note="GATase cobBQ-type"
FT   ACT_SITE        325
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000250"
FT   CONFLICT        378
FT                   /note="G -> V (in Ref. 1; BAA21090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462..483
FT                   /note="EKFTRVVRESVDVEYIIQRLGL -> REVYPGCEGER (in Ref. 1;
FT                   BAA21090)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   483 AA;  53959 MW;  FAF8D65B92DFE0D9 CRC64;
     MGKALMVQGT MSGAGKSLLV AALCRIFTNL GYDVVPFKSQ NMSLNSAPSI EGGEISRAQY
     LQALACRKKP SVKFNPILLK PEGNMRSQVV FMGRPIGSVS ARDYMLSKKA ELFEKAIEVL
     KELMREHDLV IIEGAGSPVE INLKDYDIAN MRVAKAVNAP VILVADIDRG GSFAQIVGTM
     ELLSEEEREL VMGFIFNKFR GDASLLKPGF EFLEKRCGKP VLGVVPYIEH RLPEEDSLAE
     FPKVRGDLHI QIIKLPHISN FTDFEPLHWA NGVDYVTRAE EIKGDLIIVP GSKNTVEDLL
     WMRENGIEDA IIEAHREGSF VVGICGGFQM LGKEIIDEVE SKRGRVEGIG LLPAKTVFTG
     EKRTNHLKAE VLWEPARGMW VEGYEIRMGR STSEKPFSVI TSINGARAFE PEGAIGKRAF
     GTYLHGIFHN FAFTERFLNM LRAEKGLEPV KVEEWSIEEE IEKFTRVVRE SVDVEYIIQR
     LGL