ID   COBQ_THEAC              Reviewed;         468 AA.
AC   Q9HLZ8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Probable cobyric acid synthase;
GN   Name=cobQ; OrderedLocusNames=Ta0075;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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; AL445063; CAC11223.1; -; Genomic_DNA.
DR   RefSeq; WP_010900503.1; NC_002578.1.
DR   AlphaFoldDB; Q9HLZ8; -.
DR   SMR; Q9HLZ8; -.
DR   STRING; 273075.Ta0075; -.
DR   EnsemblBacteria; CAC11223; CAC11223; CAC11223.
DR   GeneID; 1455735; -.
DR   KEGG; tac:Ta0075; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 34382at2157; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001024; 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..468
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_0000141357"
FT   DOMAIN          242..424
FT                   /note="GATase cobBQ-type"
FT   ACT_SITE        323
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  51931 MW;  CBAD6EE5D933A1E7 CRC64;
     MIQVLGTSSG SGKTTIAMAL SRIFFRSGYR VAPFKAVNMS LNSVIVEGEY EIARAQWLQA
     KAANTEPTRF MNPILLKPEG MGASQVIMLG KSLGKKTIPE YYEFIMNDGK RVIREAIDRI
     SDDYDLIIAE GAGSPAEINL LDRDMANIYV SSIYNTPAIL VGDIDRGGVF ASIYGTLSLM
     PRPDLVRWIM INKMRGDASL LEPGLKKLEN LTGKRVIGVV PYSENRLPGE DSFDYDHPRA
     RGSKITIVRY PFMENYSDLD PLVYTSTGYN YVTAENASDL SDADLIVLPG SKNVFADLEY
     MRKNGIDKII IENAGRAKIL GICGGYQMLG QRITMGEISA DGLGLLRAKT NYERTKTTRS
     VRYRVDNTLM SGTWEEGYEI HYGAVISLGG ERMNETDKGP EGNVDANRLV FGTNIHGILA
     NRSVFRFMTG RDIGEPEEYL RSEIDRFADV VKSSIDVADL IEYASSRE