ID A0A1H8DYW6_9BACL Unreviewed; 500 AA.
AC A0A1H8DYW6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=SAMN05444955_10645 {ECO:0000313|EMBL:SEN12356.1};
OS Lihuaxuella thermophila.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Lihuaxuella.
OX NCBI_TaxID=1173111 {ECO:0000313|EMBL:SEN12356.1, ECO:0000313|Proteomes:UP000199695};
RN [1] {ECO:0000313|EMBL:SEN12356.1, ECO:0000313|Proteomes:UP000199695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46701 {ECO:0000313|EMBL:SEN12356.1,
RC ECO:0000313|Proteomes:UP000199695};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOCQ01000006; SEN12356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8DYW6; -.
DR STRING; 1173111.SAMN05444955_10645; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000199695; 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:UP000199695}.
FT DOMAIN 4..228
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 255..442
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 435
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 500 AA; 55624 MW; 74682FE243B2E245 CRC64;
MKAIMLQGTA SDVGKSVLCT ALCRYFFEEG YRVAPFKSQN MALNSYVTRD GREIGRAQGV
QAEAAGIEAT VDMNPILLKP KGDLVSEVIV HGRHFADLDA GSYREQVLDQ MLEPVRQSLR
RLAREYDVLV IEGAGSPAEI NLKDRDIANM RVARMADAPV LLVADIERGG VFASIVGTLE
LLDPDERARV KGFIINKFRG SKKLLDPGIE WLEKRTGIPV LGVLPYVDLG VDPEDSMSLQ
SLELKGKQKG RADLDVAVIR LPRISNFTDF LPLMNREDVT VRYIQSVRDL EQPDVIILPG
TKNTMEDLVW LKKTGLAGEI LKLRRQGSSV VGICGGYQML GEKLTDPDAV ESDHQELDGL
GLLPMVTRFV ANKKTVRTEG TPFPEWAGPA PVEGYEIHLG RTRLTSPAVP LFQLPDGRTD
GAVAEDGAVW GTYLHGVFDN PSFTHHWINH LRRKKGLPER EELAGNRHEA REEVYAFLGH
WIREHLDLER LRAIMGLNPM
//