ID   COBQ_CARHZ              Reviewed;         497 AA.
AC   Q3AE11;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CHY_0769;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(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.
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; CP000141; ABB14396.1; -; Genomic_DNA.
DR   RefSeq; WP_011343699.1; NC_007503.1.
DR   AlphaFoldDB; Q3AE11; -.
DR   SMR; Q3AE11; -.
DR   STRING; 246194.CHY_0769; -.
DR   EnsemblBacteria; ABB14396; ABB14396; CHY_0769.
DR   KEGG; chy:CHY_0769; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002706; 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..497
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002350"
FT   DOMAIN          251..443
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   497 AA;  55828 MW;  CFF04BBAE51D917C CRC64;
     MARAIMFQGT ASHVGKSVLT LALARVLYLD GFKVAPFKAQ NMALNSYVTL DGGEMGRAQV
     AQAEACGLEP RVEMNPVLLK PSSDKGSQVI VLGKPIGHYS AKSYHLERRS MVWEAVKKAY
     ETLAQEFDFI VIEGAGSPAE VNLKASDIAN MKTAFLANAP VILVADIDRG GALASLVGTM
     ELLEPEERKM VCGFILNKFR GDLELLKPAL TFLEEKTGIP VLGVMPYIPE LLIPEEDSVS
     LEETVSNREK DLKIGVVWYP RISNFTDFEI FQYEPDVELI YIKTLQDFRD DFDLVILPGS
     KNTVADLNYL KQRGLDQKLY AYVEKGKPLI GICGGLQILG EKILDPDLVE GKETEVKALG
     ILDTVTEFRG DKITRRTSTR VTRADGYFFL QREEISGYEI HHGRTFLSGE RSDVLDNTEN
     PLVFARGRVL GTYLHGLFDN DFFRHRLLNR LRREKGLDGI ENRPTSLKNL RQENYDKIAR
     VFRENVNLKK IYEILGI