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Database: UniProt
Entry: S6CQ56_9BACT
LinkDB: S6CQ56_9BACT
Original site: S6CQ56_9BACT 
ID   S6CQ56_9BACT            Unreviewed;       500 AA.
AC   S6CQ56;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:CCG34913.1};
RN   [1] {ECO:0000313|EMBL:CCG34913.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sandrine L.;
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCG34913.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cecchini D., Laville E., Laguerre S., Robe P., Leclerc M., Dore J.,
RA   Henrissat B., Remaud-Simeon M., Monsan P., Potocki-Veronese G.;
RT   "Functional metagenomics reveals novel pathways of prebiotic breakdown by
RT   human gut bacteria.";
RL   PLoS ONE 0:0-0(2013).
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:0000256|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR   EMBL; HE717014; CCG34913.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6CQ56; -.
DR   UniPathway; UPA00148; -.
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-UniRule.
DR   CDD; cd05389; CobQ_N; 1.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00028};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00028}.
FT   DOMAIN          7..228
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          253..436
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   500 AA;  53388 MW;  5C7D3653CBEAEA0A CRC64;
     MSKAKCIMVQ GTMSGAGKSL LCAALCRIFA QDGYRVAPFK SQNMALNSFV TRDGAEMGRA
     QVVQAQAAGT EPDVRMNPIL LKPSSDVGSQ VIVNGRARGQ MSAADYFRMK RSLIPDILEA
     YNSLAAENDI IVIEGAGSPA EINLKADDIV NMGLAKLVDA PVLLAGDIDR GGVFAQLYGT
     VELLEADERA RIRGLIINKF RGDVEILRPG LAMLEEKTHL PVVGVVPYLR VEIEDEDSLS
     DRLEAKSAVK PLDIAILRLP HVSNFTDFIP LEQHPLLGVR YVQRTRQLGA PDLVILPGTK
     NTMDDLRWLR ESGLEAAVLR LSAAGTPVLG VCGGYQMLGE RLCDPAGEES GTPCTLRGLG
     LLPTTTVFGT EKHLTQTAAR AAAAPFAGAA LTGYEIHAGR TEVRGSAFCT LADGTPEGCV
     QGNVFGTYLH GLFDTGELTE KLTAFLCRKK GIDPAGADLI PMEQYRQQQF DLLADGVRAA
     LDLPAVYAAM GLAGPKGENA
//
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