ID   COBQ_PYRFU              Reviewed;         483 AA.
AC   Q8U3Z8;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PF0301;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL80425.1; -; Genomic_DNA.
DR   RefSeq; WP_011011416.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U3Z8; -.
DR   SMR; Q8U3Z8; -.
DR   STRING; 186497.PF0301; -.
DR   EnsemblBacteria; AAL80425; AAL80425; PF0301.
DR   GeneID; 41712092; -.
DR   KEGG; pfu:PF0301; -.
DR   PATRIC; fig|186497.12.peg.316; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 34382at2157; -.
DR   PhylomeDB; Q8U3Z8; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001013; 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_0000141355"
FT   DOMAIN          247..433
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        325
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   483 AA;  54538 MW;  277915AE1B35D726 CRC64;
     MGKALMIQGT MSGVGKSLIA TALCRIFSDL GYDVVPFKSQ NMSLNSAPSI EGGEISRAQY
     LQAIACRKKP SIKFNPILLK PEGNMRSQVV FLGEPIGSVS ARDYMLSKKI ELFRKSMEVL
     KSLMKRHDLV IIEGAGSPVE INLKDYDIAN MRVAREVNAP VILVADIDRG GSFAQIVGTM
     ELLSEEERNL VMGFVFNKFR GDPSLLYPGF KFLEKKYGKP VLGVVPYIDH RLPEEDSLAE
     FPRAKGEVHI QIIKLPHISN FTDFEPLHWA NGVDYVTKAE EIKGDIIIIP GSKNTVEDLI
     WMRENGIEDA IIEAHREGSF IVGICGGFQM LGEKIIDNVE SKRGEVKGIG LLPAKTIFAR
     EKRTNHLKAE VLWEPARGMR VEGYEIRFGR STTRRPFSVI KWVNGRRVEE FEGAVGERTF
     GTYLHGIFHN FEFTEAFLNL IRREKGLEPI KIREWSIEDE INRFAKIVRE SIDVDYIIEF
     LGL