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Database: UniProt
Entry: R6ZN13_9FIRM
LinkDB: R6ZN13_9FIRM
Original site: R6ZN13_9FIRM 
ID   R6ZN13_9FIRM            Unreviewed;       492 AA.
AC   R6ZN13;
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=BN699_00508 {ECO:0000313|EMBL:CDD47495.1};
OS   Firmicutes bacterium CAG:534.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263027 {ECO:0000313|EMBL:CDD47495.1, ECO:0000313|Proteomes:UP000018220};
RN   [1] {ECO:0000313|EMBL:CDD47495.1, ECO:0000313|Proteomes:UP000018220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:534 {ECO:0000313|Proteomes:UP000018220};
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|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: 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:CDD47495.1}.
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DR   EMBL; CBHC010000118; CDD47495.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6ZN13; -.
DR   STRING; 1263027.BN699_00508; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000018220; 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; 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.
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:UP000018220}.
FT   DOMAIN          5..228
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          250..433
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   492 AA;  54686 MW;  C1B72D8117F53937 CRC64;
     MAKVIMVQGT MSNAGKSLLV AGLCRVFRQD GYTVAPFKSQ NMALNSFITK EGLEMGRAQV
     MQAEAAGIAP MVCMNPILLK PISHTGSQVI VNGEVIGNMS AREYFAYKKQ LVPDIKKAFQ
     KLEEKADIIV IEGAGSPAEI NLKENDIVNM GLAEMVDAPV LLVGDIDRGG VFAQLLGTLM
     LLTKQEKDRV KGLVINKFRG DKTILDPGIL MLEEKGRVPV VGVLPYLELK LEDEDSLTER
     FDHRREGLID IAVIRYPRIS NFTDFNVFEQ NPNVTVRYVA SEEELHHPDL IILPGSKNTM
     GDLKWMRQNG MEAAVKKRVG EIPVFGICGG YQMLGEMVED PDGVEEGGAL RGMELLPVKT
     ELKKQKKRCQ VEGKIGTLPG IFSELSGCSY QGYEIHMGST HIDGEASVEW KAPVYGTRQN
     VYGSYIHGLF DQGHTAEAVV RALAKKKGLS LTEGEIQDYR KFKETQYDKL ADAMRMYFHM
     EEIYGMLREA RL
//
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