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
//