COBQ_THEON
ID COBQ_THEON Reviewed; 484 AA.
AC B6YV97;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=TON_0687;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(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; CP000855; ACJ16175.1; -; Genomic_DNA.
DR RefSeq; WP_012571647.1; NC_011529.1.
DR AlphaFoldDB; B6YV97; -.
DR STRING; 523850.TON_0687; -.
DR EnsemblBacteria; ACJ16175; ACJ16175; TON_0687.
DR GeneID; 7016988; -.
DR KEGG; ton:TON_0687; -.
DR PATRIC; fig|523850.10.peg.690; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002727; 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..484
FT /note="Probable cobyric acid synthase"
FT /id="PRO_1000090250"
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 484 AA; 53855 MW; 1A6BAF45A04B7A91 CRC64;
MGKALMVQGT SSGAGKSLLV MALCRIFSNL GYDVVPFKSQ NMSLNSAPSI EGGEISRAQY
LQAVACRKKP SVRFNPILLK PEGNMRSQVV FMGKPIGSVS AREYMLSRKE ELFRKAMKVL
DELMVEHEIV IIEGAGSPVE INLKDYDIAN MRVARHAKAK TILVTDIDRG GSFASIVGTM
ELLSKEERNL ILGFVFNKFR GDASLLEPGF EYLEKRYGKP TLGVVPCIEH KLPEEDSLTS
FPKVNGELHI QIVKLPHISN FTDFEPLHWA NGVDYVTKAE EIEGDLIIIP GSKNTVEDLL
WMRENGIEDA IIQAHHEGSF VVGICGGFQM LGEKIIDNVE SKRGEVKGIG LLPAKTIFTP
VKRTNHLKAE ILWEPAKRMS VEGYEIRMGR STSERPFSII REINGAKAFE PEGALGERTF
GTYLHGIFHN FAFTERLLNF LRAEKGLEPI SVGGWSIEEE IERFARVVEK NLDVGYIISE
LGLG