ID   A0A231R1E3_9BACL        Unreviewed;       537 AA.
AC   A0A231R1E3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=B1A99_31265 {ECO:0000313|EMBL:OXS53043.1};
OS   Cohnella sp. CIP 111063.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1955714 {ECO:0000313|EMBL:OXS53043.1, ECO:0000313|Proteomes:UP000215193};
RN   [1] {ECO:0000313|EMBL:OXS53043.1, ECO:0000313|Proteomes:UP000215193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 111063 {ECO:0000313|EMBL:OXS53043.1,
RC   ECO:0000313|Proteomes:UP000215193};
RA   Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT   "Cohnella sp SGD-V74 (T) CIP 111063, whole genome shotgun sequencing
RT   project.";
RL   Submitted (MAR-2017) 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:OXS53043.1}.
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DR   EMBL; MWSG01000028; OXS53043.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A231R1E3; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000215193; 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:UP000215193}.
FT   DOMAIN          23..250
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          274..477
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        353
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        470
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   537 AA;  59485 MW;  6F3186701F4E0F50 CRC64;
     MTQEKNAAAG SKGKRDKAIS RVLMVQGTAS DVGKSVLAAA LCRIFAQDGW TVAPFKSQNM
     SLNSYVTPDG KEIGRAQGMQ ADACGIAATT DMNPILLKPS SDRTSQVVVH GKPYKTMDAF
     SYRSEYLTEA GQIVRTALER LRAKYEIVVL EGAGSPAEIN LKDRDIVNMR MAAWADAPVL
     LAADIDRGGV FASIVGTLEL LEPEERDRVK GFVINKFRGD VELLKPGLEW LERRTGKPVV
     GVIPYLPDLR LETEDSLSFR QPAGDAQARP DRLDIVVIRL PRWSNFTDID PLLAEEDVSV
     RFAASREDFG FPDAVILPGS KNTAEDLLFL RETGLDRLIL DHRSREGWLT GICGGYQMLG
     ERLNDPEGIE SAHASLPGLA VFPMETTFGP DKKTERVTGQ AQGWSEDADA AARQTAHYDI
     EGYEIHMGRT FFTEPVSHPL LLASAESRAA SPYSEGARSQ DGRAWGTYVH GILHNDGFRR
     DWLNAIRRSK GWPPIAGELN YNRLREAEFD RLAGHVRRHL DIRKLYEMMN EGMEGSR
//