ID A0A1M4M376_9FIRM Unreviewed; 298 AA.
AC A0A1M4M376;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ1 {ECO:0000313|EMBL:SCG82139.1};
GN Synonyms=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=DW1_0528 {ECO:0000313|EMBL:SCG82139.1};
OS Proteiniborus sp. DW1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG82139.1, ECO:0000313|Proteomes:UP000185208};
RN [1] {ECO:0000313|EMBL:SCG82139.1, ECO:0000313|Proteomes:UP000185208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW1 {ECO:0000313|EMBL:SCG82139.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00028}.
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DR EMBL; FMDO01000007; SCG82139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M4M376; -.
DR STRING; 1889883.DW1_0528; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000185208; Unassembled WGS sequence.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05389; CobQ_N; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR047045; CobQ_N.
DR InterPro; IPR004459; CobQ_synth.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Ligase {ECO:0000313|EMBL:SCG82139.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185208}.
FT DOMAIN 5..228
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 298 AA; 33794 MW; 6F4AA1AECB5601A2 CRC64;
MTKNIMLQGT ASSVGKSILT AILCRILKQD GYSVAPFKSQ NMSSKSILIE DNKEISIAQA
IQAEAAMIEP NESMNPILLK PMSDIGSLVV LNGLPYKVMT ASEYHKMKLE LKWAIKEAYN
KLAQRFDIIV IEGAGSPAEI NLRDNDIVNM GLAELVDAPV ILIGDIDRGG VFASIYGTLM
LMPERERNRV KGFIINKFRG DVELLKPGIK MIEELVDKPC FGVVPYMQVD LEEEDSLIVK
NDYKEWQNPT MSMDMKQEEP SLNLQREYRE LRNREFERLA HIVRNSIDID KIKEIMRL
//
