ID   COBQ_CLOAB              Reviewed;         491 AA.
AC   Q97JB2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CA_C1374;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79342.1; -; Genomic_DNA.
DR   PIR; C97069; C97069.
DR   RefSeq; NP_348002.1; NC_003030.1.
DR   RefSeq; WP_010964683.1; NC_003030.1.
DR   AlphaFoldDB; Q97JB2; -.
DR   STRING; 272562.CA_C1374; -.
DR   DNASU; 1117557; -.
DR   EnsemblBacteria; AAK79342; AAK79342; CA_C1374.
DR   GeneID; 44997879; -.
DR   KEGG; cac:CA_C1374; -.
DR   PATRIC; fig|272562.8.peg.1579; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000814; 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; 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; 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..491
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141296"
FT   DOMAIN          246..435
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   491 AA;  54530 MW;  08D0828ED4B28840 CRC64;
     MSRIMIQGTA SSVGKSILVA ALCRIFKQDG FSVCPYKSQN MSLNSYITLD GKEMGRAQVL
     QAYAAGLEPE VYMNPILLKP TTDKSCQVIV KGEVYGVSSA KNYYNMKKEF APMLKEDFEE
     LEDKFDIVVI EGAGSPAEIN LRENDIVNMG LAELVDAPVV LVGDIDKGGV FASLFGTVML
     LEENERKRIK GTIINKFRGD VEILKPGLSM LEERINIPCF GVVPYFNLSL EDEDGAVYFN
     TKVNSKIDVA VIKLPHISNF TDIDALKIEE DVSLRYITSS ENFGTPDLLI IPGSKNTIGD
     LLYIRKNGIE NKIKQYAEKN GLIFGICGGY QMLGRLIEDP FKVETELGEI NGMGLLDIRT
     VFAEKKVTTR VQGSVIDKQI PVYGYEIHMG ISSYGEKAKP FIKIENKVGI DDGAVNEGGN
     IMGTYIHGIF DGANFREYII NFLRDKKGIE RKKSVVYEDV RNGEIDRLAD IVRNSLDMNS
     IYSVMGIEGK K