ID A0A1K1TGM2_STRAR Unreviewed; 508 AA.
AC A0A1K1TGM2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=SAMN02787144_100170 {ECO:0000313|EMBL:SFW99429.1};
OS Streptomyces atratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1893 {ECO:0000313|EMBL:SFW99429.1, ECO:0000313|Proteomes:UP000181909};
RN [1] {ECO:0000313|EMBL:SFW99429.1, ECO:0000313|Proteomes:UP000181909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK807 {ECO:0000313|EMBL:SFW99429.1,
RC ECO:0000313|Proteomes:UP000181909};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPJO01000001; SFW99429.1; -; Genomic_DNA.
DR RefSeq; WP_072483010.1; NZ_FPJO01000001.1.
DR AlphaFoldDB; A0A1K1TGM2; -.
DR STRING; 1893.SAMN02787144_100170; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000181909; 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}.
FT DOMAIN 6..235
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 262..432
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 508 AA; 54004 MW; A5BFE7C737BC92B8 CRC64;
MSGGLLVAGT TSDAGKSVVT AGICRWLVRR GVKVAPFKAQ NMSLNSFVTR EGAEIGRAQA
MQAQAARVEP SALMNPVLLK PGSDRSSQVV LMGKPVGEMS ARGYHGGRQQ ALLSTVVDCL
EQLRSTYDAV ICEGAGSPAE INLRRTDIVN MGIARAARFP VVVVGDIDRG GVFASFFGTT
ALLAAEDQSL IAGYLVNKFR GDVSLLEPGL EMLRDITGRP TYGVLPFAHG LGIDEEDGLR
VSLRGAVRES VVAPPHGEDV LRVAVCAVPL MSNFTDVDAL AAEPGVVVRF VDRAEELSDA
DLVVVPGTRG TVKALAWLRE RGLADALARR AAEGRPVLGI CGGFQVLGEH IEDEVESRAG
RVEGLGLLPV RIRFDREKTL ARPVGEALGA PVEGYEIHHG VADVHGGEPF LDGCRVGVVW
GTHWHGSLES DEFRRRFLTE VARAAGRRFV PAPDTAFAAL REEQLDRLGD LVEEHADTDA
LLRLLESGAP SGLPFIAPGA PAATGSRR
//