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Database: UniProt
Entry: R5QEP3_9FIRM
LinkDB: R5QEP3_9FIRM
Original site: R5QEP3_9FIRM 
ID   R5QEP3_9FIRM            Unreviewed;       492 AA.
AC   R5QEP3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=BN734_00892 {ECO:0000313|EMBL:CCZ27018.1};
OS   [Ruminococcus] torques CAG:61.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Mediterraneibacter.
OX   NCBI_TaxID=1263108 {ECO:0000313|EMBL:CCZ27018.1, ECO:0000313|Proteomes:UP000017998};
RN   [1] {ECO:0000313|EMBL:CCZ27018.1, ECO:0000313|Proteomes:UP000017998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:61 {ECO:0000313|Proteomes:UP000017998};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCZ27018.1}.
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DR   EMBL; CAZS010000156; CCZ27018.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QEP3; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000017998; Unassembled WGS sequence.
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; 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; PF13500; AAA_26; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017998}.
FT   DOMAIN          234..425
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        313
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   492 AA;  54373 MW;  8D9F31F8F68CFED9 CRC64;
     MLAGALCRIL KEDGYKTAPF KSQNMALNSY ITKEGLEMGR AQVMQAEAAG IEPSADMNPI
     LLKPTNDTGS QIIVRGRPFG MMSASEYYKR KKEFIPSIME SYRKLDETYD VIVIEGAGSP
     AEINLKKDDI VNMGFAKMAD APVLLVGDID RGGVFAQLAG TMLLLEEEEK KRVKGTIINK
     FRGDVSILKP GLRMLEEKIN TSVLGVIPYF HLDIEDEDSL TERFRKKSRS GLAKIAVIRL
     PRISNFTDIA PLEAVDELDV SYVSNISQFG DPDVVIIPGS KNTISDLLWM RQNGLEGKIL
     RHAAKGGIVF GICGGYQMLG QSISDPTGAE QKGTVRGMGL LPVTTVFEQE KRRTRVSGRF
     AKVGGALAEM SGVCYEGYEI HMGRTVLSKG TVPLVYMEEE GEQRQDGAQS DHVYGCYMHG
     IFDMSETVKT FLAAVLRKKG IDPSKITVRD RNAYKEEQYD RLASIVRENL NMEAVYKIIE
     KGNEASCSLL SE
//
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