ID A0A173Z8L1_9CLOT Unreviewed; 484 AA.
AC A0A173Z8L1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=CP373A1_08315 {ECO:0000313|EMBL:OBY10509.1};
OS Clostridium paraputrificum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=29363 {ECO:0000313|EMBL:OBY10509.1, ECO:0000313|Proteomes:UP000092714};
RN [1] {ECO:0000313|EMBL:OBY10509.1, ECO:0000313|Proteomes:UP000092714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=373-A1 {ECO:0000313|EMBL:OBY10509.1,
RC ECO:0000313|Proteomes:UP000092714};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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|PROSITE-ProRule:PRU00605}.
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:OBY10509.1}.
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DR EMBL; MAPZ01000019; OBY10509.1; -; Genomic_DNA.
DR RefSeq; WP_027098174.1; NZ_UAWH01000005.1.
DR AlphaFoldDB; A0A173Z8L1; -.
DR GeneID; 42776000; -.
DR eggNOG; COG1492; Bacteria.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000092714; 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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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:UP000092714}.
FT DOMAIN 7..229
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 251..432
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 484 AA; 54304 MW; 36EBAA88180AA59F CRC64;
MEAKRLMFLG TASSVGKSTL ATAFCRYYKR KGYNVAPFKA LNISLNSFVT KEGDEIGRAQ
VVQAEACEIE PKEYMNPILM KPSANNKTQV IVRGKVYCTM DGYKYKDLNK YLKGVAKEAF
DHISKDYDFI VLEGSGSCAE INLRETDIAN IEMAKVSNSP VILVADIDRG GVFASIVGTI
MLLPPEERAL IKGVIINKFR GKKEFFKPAM KQVEELINIP VLGVMPYFEL NIEDEDGVTE
KISNKKGKGI DVVVIRLPHM SNFTDFNVLR AMNGINIRYI NSPKEIENAK MIIIPGSKNT
IEDLNFIKET GFREIILEKA KSDTIIFGIC GGYQILGKEI KDPLGVEGSP REVKGLGLLD
LATTFNGKKK TRQVKAKNNE GLVVRGYEIH NGVSECLDDK SIWIQGEAGE VLGMKSRNVY
GTYLHGIFEE EDFAYTFINK YVSQLECHEK VSYKEYKMNE YDKLCDILEE NIDMDLVNSI
INGK
//
