ID A0A1V4I440_9FIRM Unreviewed; 508 AA.
AC A0A1V4I440;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN ECO:0000313|EMBL:OPJ54669.1};
GN ORFNames=CLOTH_20350 {ECO:0000313|EMBL:OPJ54669.1};
OS [Clostridium] thermoalcaliphilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=29349 {ECO:0000313|EMBL:OPJ54669.1, ECO:0000313|Proteomes:UP000190140};
RN [1] {ECO:0000313|EMBL:OPJ54669.1, ECO:0000313|Proteomes:UP000190140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7309 {ECO:0000313|EMBL:OPJ54669.1,
RC ECO:0000313|Proteomes:UP000190140};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium thermoalcaliphilum DSM 7309.";
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:OPJ54669.1}.
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DR EMBL; MZGW01000015; OPJ54669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4I440; -.
DR STRING; 29349.CLOTH_20350; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000190140; 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:UP000190140}.
FT DOMAIN 5..230
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 252..451
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 444
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 508 AA; 56874 MW; A8AC7FC4ADF98D59 CRC64;
MKKSIMFQGT GSGVGKSLIT AAFCRIFKDD GYKTVPFKSQ NMALNSFITK EGLEMGRAQV
FQAEAARIEP DVRMNPILLK PTTDKKAQVI FKGKVHKNMD AQEYHKFKPQ LENMIKEIYE
ELTSEYDICV LEGAGSPAEI NLRENDIVNM GMAKLSNSPV VLIGDIDKGG VFASLAGTMM
LLNEEERSRV KGVIINKFRG DIKILEPGLK MLEDIIKIPV LGVIPYSDIN IEDEDSLSEI
FKRRSKSNKE INIEVLYLPH VSNFTDFNVF QTQEDVNVRY VLRGESIGNP DILIIPGSKN
TIEDLIYLRE SGIEEEIKAL HKKGKLIFGI CGGYQMLGKK LYDPKGVECG IKEIDGIGFL
DIETVFEDEK VTTQVKGIIE YEGSGYLEGL KGCNIEGYEI HMGRSKLCGE SVYFDRINER
LGKITSDLEG AVNSQGNVVG TYIHGIFDNI NFTRKLLNNV RKSKGLGEIE SSVESFSEFK
EKEYNKLANI VKSNVDMNKI YEIIESGV
//
