ID A0A0N1HA44_9ACTN Unreviewed; 502 AA.
AC A0A0N1HA44;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=OV320_3227 {ECO:0000313|EMBL:KPI30443.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI30443.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI30443.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI30443.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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:KPI30443.1}.
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DR EMBL; LJCX01000022; KPI30443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1HA44; -.
DR PATRIC; fig|1592329.3.peg.2425; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000037870; 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:UP000037870}.
FT DOMAIN 6..238
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 262..431
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 341
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 502 AA; 53453 MW; 19A24F73647B42C7 CRC64;
MSGGLLVAGT TSDAGKSVVT AGICRWLVRQ GVKVAPFKAQ NMSLNSFVTR EGAEIGRAQA
MQAQAARVEP TALMNPVLLK PGSDRSSQVV LMGKPVGEMS ARGYHGGRQE QLLGTVLECL
AELRGTYDAV ICEGAGSPAE INLRRTDIVN MGVARGARLP VLVVGDIDRG GVFASFFGTV
ALLSPEDQAF VAGFLVNKFR GDVSLLEPGL DMLEGLTGRR TYGVLPFRHG LGIDEEDGLR
VSLRGSVRES EVSSPVGEDI LRVAVCAIPL MSNFTDVDAL AAEPGVVVRF VDRAEELVDA
DLVVVPGTRG TVRALEWMRE RGLADALARR AAEGRPVLGI CGGFQILGEH IEDEVESRAG
QVDGLGLLPV RVRFAREKTL TRPVGEALGE PVEGYEIHHG VAQVTGGKPF LDGCRVGEVW
GTHWHGSLES DGFRRAFLRE VAAAAGRRFV PAADTSFGSL REEQLDRLGD LIEEHADTDA
LWRLIESGAP TGLPFIPPGA PA
//
